P15529 (MCP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Membrane cofactor protein

Alternative name(s):
TLX
Trophoblast leukocyte common antigen
CD_antigen=CD46

Gene names

Name:	CD46
Synonyms:	MCP, MIC10

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	392 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts as a cofactor for complement factor I, a serine protease which protects autologous cells against complement-mediated injury by cleaving C3b and C4b deposited on host tissue. May be involved in the fusion of the spermatozoa with the oocyte during fertilization. Also acts as a costimulatory factor for T-cells which induces the differentiation of CD4+ into T-regulatory 1 cells. T-regulatory 1 cells suppress immune responses by secreting interleukin-10, and therefore are thought to prevent autoimmunity. A number of viral and bacterial pathogens seem to exploit this property and directly induce an immunosuppressive phenotype in T-cells by binding to CD46. Ref.29 Ref.41
Subunit structure	Interacts with C3b and C4b. Binds to Measles virus H protein, to Human herpesvirus 6 GH protein and to human adenovirus B/D PIV/fiber protein, and acts as a receptor for these viruses. Binds to Streptococcus pyogenes M protein and to type IV pili from Neisseria, and may act as a receptor for these pathogenic bacteria. Ref.1 Ref.19 Ref.23 Ref.25 Ref.30 Ref.31 Ref.34 Ref.36 Ref.38 Ref.39 Ref.42 Ref.44 Ref.45 Ref.46 Ref.47
Subcellular location	Cytoplasmic vesicle › secretory vesicle › acrosome inner membrane; Single-pass type I membrane protein. Note: Inner acrosomal membrane of spermatozoa. Internalized upon binding of Measles virus, Herpesvirus 6 or Neisseria gonorrhoeae, which results in an increased susceptibility of infected cells to complement-mediated injury. In cancer cells or cells infected by Neisseria, shedding leads to a soluble peptide. Ref.35 Ref.37 Ref.43
Tissue specificity	Expressed by all cells except erythrocytes.
Domain	Sushi domains 1 and 2 are required for interaction with human adenovirus B PIV/FIBER protein and with Measles virus H protein. Sushi domains 2 and 3 are required for Herpesvirus 6 binding. Sushi domain 3 is required for Neisseria binding. Sushi domains 3 and 4 are required for interaction with Streptococcus pyogenes M protein and are the most important for interaction with C3b and C4b.
Post-translational modification	N-glycosylated on Asn-83; Asn-114 and Asn-273 in most tissues, but probably less N-glycosylated in testis. N-glycosylation on Asn-114 and Asn-273 is required for cytoprotective function. N-glycosylation on Asn-114 is required for Measles virus binding. N-glycosylation on Asn-273 is required for Neisseria binding. N-glycosylation is not required for human adenovirus binding. Ref.35 Ref.43 Extensively O-glycosylated in the Ser/Thr-rich domain. O-glycosylation is required for Neisseria binding but not for Measles virus or human adenovirus binding. Ref.35 Ref.43 In epithelial cells, isoforms B/D/F/H/J/L/3 are phosphorylated by YES1 in response to infection by Neisseria gonorrhoeae; which promotes infectivity. In T-cells, these isoforms may be phosphorylated by Lck. Ref.28 Ref.33
Involvement in disease	Hemolytic uremic syndrome atypical 2 (AHUS2) [MIM:612922]: An atypical form of hemolytic uremic syndrome. It is a complex genetic disease characterized by microangiopathic hemolytic anemia, thrombocytopenia, renal failure and absence of episodes of enterocolitis and diarrhea. In contrast to typical hemolytic uremic syndrome, atypical forms have a poorer prognosis, with higher death rates and frequent progression to end-stage renal disease. Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Other genes may play a role in modifying the phenotype. Patients with CD46 mutations seem to have an overall better prognosis compared to patients carrying CFH mutations. Ref.40 Ref.49 Ref.50 Ref.51 Ref.53
Sequence similarities	Contains 4 Sushi (CCP/SCR) domains.

Ontologies

Keywords
Biological process	Complement pathway Fertilization Host-virus interaction Immunity Innate immunity
Cellular component	Cytoplasmic vesicle Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Hemolytic uremic syndrome
Domain	Repeat Signal Sushi Transmembrane Transmembrane helix
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	complement activation, classical pathway Inferred from electronic annotation. Source: UniProtKB-KW innate immune response Traceable author statement. Source: Reactome negative regulation of complement activation Inferred from electronic annotation. Source: Compara proteolysis Inferred from electronic annotation. Source: Compara regulation of complement activation Traceable author statement. Source: Reactome single fertilization Inferred from electronic annotation. Source: UniProtKB-KW virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: Compara basolateral plasma membrane Inferred from electronic annotation. Source: Compara cell surface Inferred from electronic annotation. Source: Compara inner acrosomal membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to plasma membrane Traceable author statement Ref.3. Source: ProtInc
Molecular_function	receptor activity Traceable author statement Ref.21. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 16 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist. The complete sequences of the isoforms are not known. Isoforms are classified as alpha (isoform C and isoform D), beta (isoform E and isoform F), gamma (isoform A and isoform B) and delta (isoform N). Isoforms gamma are preferentially expressed in EBV-B cells and leukemic cells. Isoforms alpha (66 kDa) and isoforms beta (56 kDa) are found in all tissues except sperm. Isoform delta is expressed in spermatozoa. The exon 9 is specifically deleted in some placentae isoforms. All tissues differentially splice exon 13.

Isoform A (identifier: P15529-1)

Also known as: no del; ABC1;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform B (identifier: P15529-2)

Also known as: del 13; ABC2;

The sequence of this isoform differs from the canonical sequence as follows:
     377-392: TYLTDETHREVKFTSL → KADGGAEYATYQTKSTTPAEQRG

Note: Contains a phosphotyrosine at position 384. Contains a phosphotyrosine at position 387.

Isoform C (identifier: P15529-11)

Also known as: del 7; BC1;

The sequence of this isoform differs from the canonical sequence as follows:
     286-300: Missing.

Isoform D (identifier: P15529-3)

Also known as: del 7-13; BC2;

The sequence of this isoform differs from the canonical sequence as follows:
     286-300: Missing.
     377-392: TYLTDETHREVKFTSL → KADGGAEYATYQTKSTTPAEQRG

Note: Contains a phosphotyrosine at position 369. Contains a phosphotyrosine at position 372.

Isoform E (identifier: P15529-12)

Also known as: del 7-8; C1;

The sequence of this isoform differs from the canonical sequence as follows:
     286-315: Missing.

Isoform F (identifier: P15529-4)

Also known as: del 7-8-13; C2;

The sequence of this isoform differs from the canonical sequence as follows:
     286-315: Missing.
     377-392: TYLTDETHREVKFTSL → KADGGAEYATYQTKSTTPAEQRG

Note: Contains a phosphotyrosine at position 354. Contains a phosphotyrosine at position 357.

Isoform G (identifier: P15529-13)

Also known as: del 9;

The sequence of this isoform differs from the canonical sequence as follows:
     316-329: Missing.

Isoform H (identifier: P15529-5)

Also known as: del 9-13;

The sequence of this isoform differs from the canonical sequence as follows:
     316-329: Missing.
     377-392: TYLTDETHREVKFTSL → KADGGAEYATYQTKSTTPAEQRG

Note: Contains a phosphotyrosine at position 370. Contains a phosphotyrosine at position 373.

Isoform I (identifier: P15529-14)

Also known as: del 7-9;

The sequence of this isoform differs from the canonical sequence as follows:
     286-300: Missing.
     316-329: Missing.

Isoform J (identifier: P15529-6)

Also known as: del 7-9-13;

The sequence of this isoform differs from the canonical sequence as follows:
     286-300: Missing.
     316-329: Missing.
     377-392: TYLTDETHREVKFTSL → KADGGAEYATYQTKSTTPAEQRG

Note: Contains a phosphotyrosine at position 355. Contains a phosphotyrosine at position 358.

Isoform K (identifier: P15529-15)

Also known as: del 7-8-9;

The sequence of this isoform differs from the canonical sequence as follows:
     286-329: Missing.

Isoform L (identifier: P15529-7)

Also known as: del 7-8-9-13;

The sequence of this isoform differs from the canonical sequence as follows:
     286-329: Missing.
     377-392: TYLTDETHREVKFTSL → KADGGAEYATYQTKSTTPAEQRG

Isoform M (identifier: P15529-8)

Also known as: del 7-12a-13;

The sequence of this isoform differs from the canonical sequence as follows:
     286-300: Missing.
     355-367: Missing.
     368-392: YLQRRKKKGTYLTDETHREVKFTSL → GKQMVELNMPLTRLNQPLQQSREAE

Isoform N (identifier: P15529-9)

Also known as: del 7-8-12-13;

The sequence of this isoform differs from the canonical sequence as follows:
     286-315: Missing.
     355-392: VVGVAVICVVPYRYLQRRKKKGTYLTDETHREVKFTSL → GKQMVELNMPLTRLNQPLQQSREAE

Note: No experimental confirmation available.

Isoform 2 (identifier: P15529-10)

The sequence of this isoform differs from the canonical sequence as follows:
     301-305: Missing.

Isoform 3 (identifier: P15529-16)

The sequence of this isoform differs from the canonical sequence as follows:
     33-33: D → G
     34-96: Missing.
     377-392: TYLTDETHREVKFTSL → KADGGAEYATYQTKSTTPAEQRG

Note: Contains a phosphotyrosine at position 321. Contains a phosphotyrosine at position 324.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 34

34

Ref.1 Ref.16 Ref.17 Ref.18

Chain

35 – 392

358

Membrane cofactor protein

PRO_0000006008

Regions

Topological domain

35 – 343

309

Extracellular Potential

Transmembrane

344 – 366

23

Helical; Potential

Topological domain

367 – 392

26

Cytoplasmic Potential

Domain

35 – 96

62

Sushi 1

Domain

97 – 159

63

Sushi 2

Domain

160 – 225

66

Sushi 3

Domain

226 – 285

60

Sushi 4

Compositional bias

302 – 326

25

Ser/Thr-rich

Amino acid modifications

Glycosylation

83

1

N-linked (GlcNAc...)

Glycosylation

114

1

N-linked (GlcNAc...)

Glycosylation

163

1

O-linked (GalNAc...) Potential

Glycosylation

273

1

N-linked (GlcNAc...)

Glycosylation

290

1

O-linked (GalNAc...) Potential

Glycosylation

291

1

O-linked (GalNAc...) Potential

Glycosylation

292

1

O-linked (GalNAc...) Potential

Glycosylation

298

1

O-linked (GalNAc...) Potential

Glycosylation

300

1

O-linked (GalNAc...) Potential

Glycosylation

302

1

O-linked (GalNAc...) Potential

Glycosylation

303

1

O-linked (GalNAc...) Potential

Glycosylation

304

1

O-linked (GalNAc...) Potential

Glycosylation

305

1

O-linked (GalNAc...) Potential

Glycosylation

306

1

O-linked (GalNAc...) Potential

Glycosylation

307

1

O-linked (GalNAc...) Potential

Glycosylation

309

1

O-linked (GalNAc...) Potential

Glycosylation

312

1

O-linked (GalNAc...) Potential

Glycosylation

313

1

O-linked (GalNAc...) Potential

Glycosylation

315

1

O-linked (GalNAc...) Potential

Glycosylation

320

1

O-linked (GalNAc...) Potential

Glycosylation

326

1

O-linked (GalNAc...) Potential

Disulfide bond

35 ↔ 80

By similarity

Disulfide bond

64 ↔ 94

By similarity

Disulfide bond

99 ↔ 141

By similarity

Disulfide bond

127 ↔ 157

By similarity

Disulfide bond

162 ↔ 210

By similarity

Disulfide bond

191 ↔ 223

By similarity

Disulfide bond

228 ↔ 270

By similarity

Disulfide bond

256 ↔ 283

By similarity

Natural variations

Alternative sequence

33

1

D → G in isoform 3.

VSP_019005

Alternative sequence

34 – 96

63

Missing in isoform 3.

VSP_019006

Alternative sequence

286 – 329

44

Missing in isoform K and isoform L.

VSP_009176

Alternative sequence

286 – 315

30

Missing in isoform E, isoform F and isoform N.

VSP_009175

Alternative sequence

286 – 300

15

Missing in isoform C, isoform D, isoform I, isoform J and isoform M.

VSP_009174

Alternative sequence

301 – 305

5

Missing in isoform 2.

VSP_001201

Alternative sequence

316 – 329

14

Missing in isoform G, isoform H, isoform I and isoform J.

VSP_009177

Alternative sequence

355 – 392

38

VVGVA…KFTSL → GKQMVELNMPLTRLNQPLQQ SREAE in isoform N.

VSP_009178

Alternative sequence

355 – 367

13

Missing in isoform M.

VSP_001202

Alternative sequence

368 – 392

25

YLQRR…KFTSL → GKQMVELNMPLTRLNQPLQQ SREAE in isoform M.

VSP_001203

Alternative sequence

377 – 392

16

TYLTD…KFTSL → KADGGAEYATYQTKSTTPAE QRG in isoform B, isoform D, isoform F, isoform H, isoform J, isoform L and isoform 3.

VSP_001204

Natural variant

13

1

S → F. Ref.9 Ref.14

VAR_026567

Natural variant

35

1

C → Y in AHUS2. Ref.50

VAR_063656

Natural variant

59

1

R → Q. Ref.14

VAR_026568

Natural variant

165

1

P → S in AHUS2; reduced cell surface expression. Ref.51

VAR_026569

Natural variant

216

1

W → C in AHUS2. Ref.53

VAR_063657

Natural variant

228

1

C → Y in a colorectal cancer sample; somatic mutation. Ref.52

VAR_035828

Natural variant

231

1

P → R in AHUS2. Ref.53

VAR_063658

Natural variant

240

1

S → P in AHUS2; no change in cell surface expression but reduced activity. Ref.49

VAR_026570

Natural variant

266

1

D → N. Ref.10
Corresponds to variant rs17006830 [ dbSNP | Ensembl ].

VAR_022262

Natural variant

271 – 272

2

Missing in AHUS2; no cell surface expression.

VAR_026571

Natural variant

324

1

P → L. Ref.10
Corresponds to variant rs41317833 [ dbSNP | Ensembl ].

VAR_022263

Natural variant

353

1

A → V. Ref.10 Ref.52
Corresponds to variant rs35366573 [ dbSNP | Ensembl ].

VAR_022264

Natural variant

355

1

V → G. Ref.10

VAR_022265

Experimental info

Mutagenesis

83

1

N → Q: No effect on cytoprotective function. No effect on Neisseria binding. No effect on Measles virus binding. Ref.24 Ref.26 Ref.31

Mutagenesis

114

1

N → Q: Strongly decreases cytoprotective function. Decreases Neisseria binding. Abolishes Measles virus binding. Ref.24 Ref.26 Ref.31

Mutagenesis

273

1

N → Q: Strongly decreases cytoprotective function. Abolishes Neisseria binding. No effect on Measles virus binding. Ref.24 Ref.26 Ref.31

Sequence conflict

25

1

V → A in CAE45719. Ref.8

Sequence conflict

108

1

G → S in CAD97694. Ref.8

Sequence conflict

159

1

K → S in CAD97694. Ref.8

Sequence conflict

162

1

C → R in CAI45983. Ref.8

Secondary structure

1

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392

Helix Strand Turn

Details...

Beta strand

42 – 48

7

Beta strand

59 – 64

6

Beta strand

68 – 70

3

Beta strand

72 – 74

3

Beta strand

77 – 80

4

Beta strand

84 – 86

3

Helix

91 – 93

3

Beta strand

94 – 96

3

Beta strand

108 – 112

5

Beta strand

115 – 118

4

Beta strand

122 – 127

6

Beta strand

131 – 135

5

Beta strand

137 – 146

10

Beta strand

148 – 152

5

Beta strand

156 – 159

4

Beta strand

171 – 175

5

Beta strand

186 – 191

6

Beta strand

195 – 198

4

Beta strand

201 – 204

4

Beta strand

206 – 210

5

Beta strand

214 – 218

5

Beta strand

222 – 224

3

Beta strand

236 – 240

5

Beta strand

251 – 256

6

Beta strand

260 – 264

5

Beta strand

266 – 270

5

Beta strand

276 – 278

3

Beta strand

282 – 285

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform A (no del) (ABC1) [UniParc]. Last modified January 16, 2004. Version 3. Checksum: 85FE0CF100EA703E	FASTA	392	43,747
	10 20 30 40 50 60 MEPPGRRECP FPSWRFPGLL LAAMVLLLYS FSDACEEPPT FEAMELIGKP KPYYEIGERV 70 80 90 100 110 120 DYKCKKGYFY IPPLATHTIC DRNHTWLPVS DDACYRETCP YIRDPLNGQA VPANGTYEFG 130 140 150 160 170 180 YQMHFICNEG YYLIGEEILY CELKGSVAIW SGKPPICEKV LCTPPPKIKN GKHTFSEVEV 190 200 210 220 230 240 FEYLDAVTYS CDPAPGPDPF SLIGESTIYC GDNSVWSRAA PECKVVKCRF PVVENGKQIS 250 260 270 280 290 300 GFGKKFYYKA TVMFECDKGF YLDGSDTIVC DSNSTWDPPV PKCLKVLPPS STKPPALSHS 310 320 330 340 350 360 VSTSSTTKSP ASSASGPRPT YKPPVSNYPG YPKPEEGILD SLDVWVIAVI VIAIVVGVAV 370 380 390 ICVVPYRYLQ RRKKKGTYLT DETHREVKFT SL
	Isoform B (del 13) (ABC2) [UniParc]. Checksum: 8E4C641F2BD8AC15	FASTA	399	44,238
	10 20 30 40 50 60 MEPPGRRECP FPSWRFPGLL LAAMVLLLYS FSDACEEPPT FEAMELIGKP KPYYEIGERV 70 80 90 100 110 120 DYKCKKGYFY IPPLATHTIC DRNHTWLPVS DDACYRETCP YIRDPLNGQA VPANGTYEFG 130 140 150 160 170 180 YQMHFICNEG YYLIGEEILY CELKGSVAIW SGKPPICEKV LCTPPPKIKN GKHTFSEVEV 190 200 210 220 230 240 FEYLDAVTYS CDPAPGPDPF SLIGESTIYC GDNSVWSRAA PECKVVKCRF PVVENGKQIS 250 260 270 280 290 300 GFGKKFYYKA TVMFECDKGF YLDGSDTIVC DSNSTWDPPV PKCLKVLPPS STKPPALSHS 310 320 330 340 350 360 VSTSSTTKSP ASSASGPRPT YKPPVSNYPG YPKPEEGILD SLDVWVIAVI VIAIVVGVAV 370 380 390 ICVVPYRYLQ RRKKKGKADG GAEYATYQTK STTPAEQRG
	Isoform C (del 7) (BC1) [UniParc]. Checksum: 2CA6F61752570B57	FASTA	377	42,248
	10 20 30 40 50 60 MEPPGRRECP FPSWRFPGLL LAAMVLLLYS FSDACEEPPT FEAMELIGKP KPYYEIGERV 70 80 90 100 110 120 DYKCKKGYFY IPPLATHTIC DRNHTWLPVS DDACYRETCP YIRDPLNGQA VPANGTYEFG 130 140 150 160 170 180 YQMHFICNEG YYLIGEEILY CELKGSVAIW SGKPPICEKV LCTPPPKIKN GKHTFSEVEV 190 200 210 220 230 240 FEYLDAVTYS CDPAPGPDPF SLIGESTIYC GDNSVWSRAA PECKVVKCRF PVVENGKQIS 250 260 270 280 290 300 GFGKKFYYKA TVMFECDKGF YLDGSDTIVC DSNSTWDPPV PKCLKVSTSS TTKSPASSAS 310 320 330 340 350 360 GPRPTYKPPV SNYPGYPKPE EGILDSLDVW VIAVIVIAIV VGVAVICVVP YRYLQRRKKK 370 GTYLTDETHR EVKFTSL
	Isoform D (del 7-13) (BC2) [UniParc]. Checksum: F45B03CBB466AA8C	FASTA	384	42,738
	10 20 30 40 50 60 MEPPGRRECP FPSWRFPGLL LAAMVLLLYS FSDACEEPPT FEAMELIGKP KPYYEIGERV 70 80 90 100 110 120 DYKCKKGYFY IPPLATHTIC DRNHTWLPVS DDACYRETCP YIRDPLNGQA VPANGTYEFG 130 140 150 160 170 180 YQMHFICNEG YYLIGEEILY CELKGSVAIW SGKPPICEKV LCTPPPKIKN GKHTFSEVEV 190 200 210 220 230 240 FEYLDAVTYS CDPAPGPDPF SLIGESTIYC GDNSVWSRAA PECKVVKCRF PVVENGKQIS 250 260 270 280 290 300 GFGKKFYYKA TVMFECDKGF YLDGSDTIVC DSNSTWDPPV PKCLKVSTSS TTKSPASSAS 310 320 330 340 350 360 GPRPTYKPPV SNYPGYPKPE EGILDSLDVW VIAVIVIAIV VGVAVICVVP YRYLQRRKKK 370 380 GKADGGAEYA TYQTKSTTPA EQRG
	Isoform E (del 7-8) (C1) [UniParc]. Checksum: AA3F3F3110E8727D	FASTA	362	40,868
	10 20 30 40 50 60 MEPPGRRECP FPSWRFPGLL LAAMVLLLYS FSDACEEPPT FEAMELIGKP KPYYEIGERV 70 80 90 100 110 120 DYKCKKGYFY IPPLATHTIC DRNHTWLPVS DDACYRETCP YIRDPLNGQA VPANGTYEFG 130 140 150 160 170 180 YQMHFICNEG YYLIGEEILY CELKGSVAIW SGKPPICEKV LCTPPPKIKN GKHTFSEVEV 190 200 210 220 230 240 FEYLDAVTYS CDPAPGPDPF SLIGESTIYC GDNSVWSRAA PECKVVKCRF PVVENGKQIS 250 260 270 280 290 300 GFGKKFYYKA TVMFECDKGF YLDGSDTIVC DSNSTWDPPV PKCLKGPRPT YKPPVSNYPG 310 320 330 340 350 360 YPKPEEGILD SLDVWVIAVI VIAIVVGVAV ICVVPYRYLQ RRKKKGTYLT DETHREVKFT SL
	Isoform F (del 7-8-13) (C2) [UniParc]. Checksum: 3BD3000428BBA2EA	FASTA	369	41,359
	10 20 30 40 50 60 MEPPGRRECP FPSWRFPGLL LAAMVLLLYS FSDACEEPPT FEAMELIGKP KPYYEIGERV 70 80 90 100 110 120 DYKCKKGYFY IPPLATHTIC DRNHTWLPVS DDACYRETCP YIRDPLNGQA VPANGTYEFG 130 140 150 160 170 180 YQMHFICNEG YYLIGEEILY CELKGSVAIW SGKPPICEKV LCTPPPKIKN GKHTFSEVEV 190 200 210 220 230 240 FEYLDAVTYS CDPAPGPDPF SLIGESTIYC GDNSVWSRAA PECKVVKCRF PVVENGKQIS 250 260 270 280 290 300 GFGKKFYYKA TVMFECDKGF YLDGSDTIVC DSNSTWDPPV PKCLKGPRPT YKPPVSNYPG 310 320 330 340 350 360 YPKPEEGILD SLDVWVIAVI VIAIVVGVAV ICVVPYRYLQ RRKKKGKADG GAEYATYQTK STTPAEQRG
	Isoform G (del 9) [UniParc]. Checksum: AE60F628C4DC271C	FASTA	378	42,193
	10 20 30 40 50 60 MEPPGRRECP FPSWRFPGLL LAAMVLLLYS FSDACEEPPT FEAMELIGKP KPYYEIGERV 70 80 90 100 110 120 DYKCKKGYFY IPPLATHTIC DRNHTWLPVS DDACYRETCP YIRDPLNGQA VPANGTYEFG 130 140 150 160 170 180 YQMHFICNEG YYLIGEEILY CELKGSVAIW SGKPPICEKV LCTPPPKIKN GKHTFSEVEV 190 200 210 220 230 240 FEYLDAVTYS CDPAPGPDPF SLIGESTIYC GDNSVWSRAA PECKVVKCRF PVVENGKQIS 250 260 270 280 290 300 GFGKKFYYKA TVMFECDKGF YLDGSDTIVC DSNSTWDPPV PKCLKVLPPS STKPPALSHS 310 320 330 340 350 360 VSTSSTTKSP ASSASGYPKP EEGILDSLDV WVIAVIVIAI VVGVAVICVV PYRYLQRRKK 370 KGTYLTDETH REVKFTSL
	Isoform H (del 9-13) [UniParc]. Checksum: 45FB279DC30B895E	FASTA	385	42,683
	10 20 30 40 50 60 MEPPGRRECP FPSWRFPGLL LAAMVLLLYS FSDACEEPPT FEAMELIGKP KPYYEIGERV 70 80 90 100 110 120 DYKCKKGYFY IPPLATHTIC DRNHTWLPVS DDACYRETCP YIRDPLNGQA VPANGTYEFG 130 140 150 160 170 180 YQMHFICNEG YYLIGEEILY CELKGSVAIW SGKPPICEKV LCTPPPKIKN GKHTFSEVEV 190 200 210 220 230 240 FEYLDAVTYS CDPAPGPDPF SLIGESTIYC GDNSVWSRAA PECKVVKCRF PVVENGKQIS 250 260 270 280 290 300 GFGKKFYYKA TVMFECDKGF YLDGSDTIVC DSNSTWDPPV PKCLKVLPPS STKPPALSHS 310 320 330 340 350 360 VSTSSTTKSP ASSASGYPKP EEGILDSLDV WVIAVIVIAI VVGVAVICVV PYRYLQRRKK 370 380 KGKADGGAEY ATYQTKSTTP AEQRG
	Isoform I (del 7-9) [UniParc]. Checksum: E48C0E7C0A616FF1	FASTA	363	40,693
	10 20 30 40 50 60 MEPPGRRECP FPSWRFPGLL LAAMVLLLYS FSDACEEPPT FEAMELIGKP KPYYEIGERV 70 80 90 100 110 120 DYKCKKGYFY IPPLATHTIC DRNHTWLPVS DDACYRETCP YIRDPLNGQA VPANGTYEFG 130 140 150 160 170 180 YQMHFICNEG YYLIGEEILY CELKGSVAIW SGKPPICEKV LCTPPPKIKN GKHTFSEVEV 190 200 210 220 230 240 FEYLDAVTYS CDPAPGPDPF SLIGESTIYC GDNSVWSRAA PECKVVKCRF PVVENGKQIS 250 260 270 280 290 300 GFGKKFYYKA TVMFECDKGF YLDGSDTIVC DSNSTWDPPV PKCLKVSTSS TTKSPASSAS 310 320 330 340 350 360 GYPKPEEGIL DSLDVWVIAV IVIAIVVGVA VICVVPYRYL QRRKKKGTYL TDETHREVKF TSL
	Isoform J (del 7-9-13) [UniParc]. Checksum: CC2FD6E11C9A81E4	FASTA	370	41,183
	10 20 30 40 50 60 MEPPGRRECP FPSWRFPGLL LAAMVLLLYS FSDACEEPPT FEAMELIGKP KPYYEIGERV 70 80 90 100 110 120 DYKCKKGYFY IPPLATHTIC DRNHTWLPVS DDACYRETCP YIRDPLNGQA VPANGTYEFG 130 140 150 160 170 180 YQMHFICNEG YYLIGEEILY CELKGSVAIW SGKPPICEKV LCTPPPKIKN GKHTFSEVEV 190 200 210 220 230 240 FEYLDAVTYS CDPAPGPDPF SLIGESTIYC GDNSVWSRAA PECKVVKCRF PVVENGKQIS 250 260 270 280 290 300 GFGKKFYYKA TVMFECDKGF YLDGSDTIVC DSNSTWDPPV PKCLKVSTSS TTKSPASSAS 310 320 330 340 350 360 GYPKPEEGIL DSLDVWVIAV IVIAIVVGVA VICVVPYRYL QRRKKKGKAD GGAEYATYQT 370 KSTTPAEQRG
	Isoform K (del 7-8-9) [UniParc]. Checksum: A6F0D0E7C4203DDF	FASTA	348	39,313
	10 20 30 40 50 60 MEPPGRRECP FPSWRFPGLL LAAMVLLLYS FSDACEEPPT FEAMELIGKP KPYYEIGERV 70 80 90 100 110 120 DYKCKKGYFY IPPLATHTIC DRNHTWLPVS DDACYRETCP YIRDPLNGQA VPANGTYEFG 130 140 150 160 170 180 YQMHFICNEG YYLIGEEILY CELKGSVAIW SGKPPICEKV LCTPPPKIKN GKHTFSEVEV 190 200 210 220 230 240 FEYLDAVTYS CDPAPGPDPF SLIGESTIYC GDNSVWSRAA PECKVVKCRF PVVENGKQIS 250 260 270 280 290 300 GFGKKFYYKA TVMFECDKGF YLDGSDTIVC DSNSTWDPPV PKCLKGYPKP EEGILDSLDV 310 320 330 340 WVIAVIVIAI VVGVAVICVV PYRYLQRRKK KGTYLTDETH REVKFTSL
	Isoform L (del 7-8-9-13) [UniParc]. Checksum: 86C83A0D515EDF86	FASTA	355	39,804
	10 20 30 40 50 60 MEPPGRRECP FPSWRFPGLL LAAMVLLLYS FSDACEEPPT FEAMELIGKP KPYYEIGERV 70 80 90 100 110 120 DYKCKKGYFY IPPLATHTIC DRNHTWLPVS DDACYRETCP YIRDPLNGQA VPANGTYEFG 130 140 150 160 170 180 YQMHFICNEG YYLIGEEILY CELKGSVAIW SGKPPICEKV LCTPPPKIKN GKHTFSEVEV 190 200 210 220 230 240 FEYLDAVTYS CDPAPGPDPF SLIGESTIYC GDNSVWSRAA PECKVVKCRF PVVENGKQIS 250 260 270 280 290 300 GFGKKFYYKA TVMFECDKGF YLDGSDTIVC DSNSTWDPPV PKCLKGYPKP EEGILDSLDV 310 320 330 340 350 WVIAVIVIAI VVGVAVICVV PYRYLQRRKK KGKADGGAEY ATYQTKSTTP AEQRG
	Isoform M (del 7-12a-13) [UniParc]. Checksum: B09E917D96F2C0DC	FASTA	364	40,705
	10 20 30 40 50 60 MEPPGRRECP FPSWRFPGLL LAAMVLLLYS FSDACEEPPT FEAMELIGKP KPYYEIGERV 70 80 90 100 110 120 DYKCKKGYFY IPPLATHTIC DRNHTWLPVS DDACYRETCP YIRDPLNGQA VPANGTYEFG 130 140 150 160 170 180 YQMHFICNEG YYLIGEEILY CELKGSVAIW SGKPPICEKV LCTPPPKIKN GKHTFSEVEV 190 200 210 220 230 240 FEYLDAVTYS CDPAPGPDPF SLIGESTIYC GDNSVWSRAA PECKVVKCRF PVVENGKQIS 250 260 270 280 290 300 GFGKKFYYKA TVMFECDKGF YLDGSDTIVC DSNSTWDPPV PKCLKVSTSS TTKSPASSAS 310 320 330 340 350 360 GPRPTYKPPV SNYPGYPKPE EGILDSLDVW VIAVIVIAIG KQMVELNMPL TRLNQPLQQS REAE
	Isoform N (del 7-8-12-13) [UniParc]. Checksum: 8EFCEDA30D3C818E	FASTA	349	39,325
	10 20 30 40 50 60 MEPPGRRECP FPSWRFPGLL LAAMVLLLYS FSDACEEPPT FEAMELIGKP KPYYEIGERV 70 80 90 100 110 120 DYKCKKGYFY IPPLATHTIC DRNHTWLPVS DDACYRETCP YIRDPLNGQA VPANGTYEFG 130 140 150 160 170 180 YQMHFICNEG YYLIGEEILY CELKGSVAIW SGKPPICEKV LCTPPPKIKN GKHTFSEVEV 190 200 210 220 230 240 FEYLDAVTYS CDPAPGPDPF SLIGESTIYC GDNSVWSRAA PECKVVKCRF PVVENGKQIS 250 260 270 280 290 300 GFGKKFYYKA TVMFECDKGF YLDGSDTIVC DSNSTWDPPV PKCLKGPRPT YKPPVSNYPG 310 320 330 340 YPKPEEGILD SLDVWVIAVI VIAIGKQMVE LNMPLTRLNQ PLQQSREAE
	Isoform 2 [UniParc]. Checksum: 20E7721BB47CA27C	FASTA	387	43,286
	10 20 30 40 50 60 MEPPGRRECP FPSWRFPGLL LAAMVLLLYS FSDACEEPPT FEAMELIGKP KPYYEIGERV 70 80 90 100 110 120 DYKCKKGYFY IPPLATHTIC DRNHTWLPVS DDACYRETCP YIRDPLNGQA VPANGTYEFG 130 140 150 160 170 180 YQMHFICNEG YYLIGEEILY CELKGSVAIW SGKPPICEKV LCTPPPKIKN GKHTFSEVEV 190 200 210 220 230 240 FEYLDAVTYS CDPAPGPDPF SLIGESTIYC GDNSVWSRAA PECKVVKCRF PVVENGKQIS 250 260 270 280 290 300 GFGKKFYYKA TVMFECDKGF YLDGSDTIVC DSNSTWDPPV PKCLKVLPPS STKPPALSHS 310 320 330 340 350 360 TTKSPASSAS GPRPTYKPPV SNYPGYPKPE EGILDSLDVW VIAVIVIAIV VGVAVICVVP 370 380 YRYLQRRKKK GTYLTDETHR EVKFTSL
	Isoform 3 [UniParc]. Checksum: F57541078036A7EA	FASTA	336	36,826
	10 20 30 40 50 60 MEPPGRRECP FPSWRFPGLL LAAMVLLLYS FSGETCPYIR DPLNGQAVPA NGTYEFGYQM 70 80 90 100 110 120 HFICNEGYYL IGEEILYCEL KGSVAIWSGK PPICEKVLCT PPPKIKNGKH TFSEVEVFEY 130 140 150 160 170 180 LDAVTYSCDP APGPDPFSLI GESTIYCGDN SVWSRAAPEC KVVKCRFPVV ENGKQISGFG 190 200 210 220 230 240 KKFYYKATVM FECDKGFYLD GSDTIVCDSN STWDPPVPKC LKVLPPSSTK PPALSHSVST 250 260 270 280 290 300 SSTTKSPASS ASGPRPTYKP PVSNYPGYPK PEEGILDSLD VWVIAVIVIA IVVGVAVICV 310 320 330 VPYRYLQRRK KKGKADGGAE YATYQTKSTT PAEQRG

References

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[1]	"Molecular cloning and chromosomal localization of human membrane cofactor protein (MCP). Evidence for inclusion in the multigene family of complement-regulatory proteins." Lublin D.M., Liszewski M.K., Post T.W., Arce M.A., le Beau M.M., Rebentisch M.B., Lemons R.S., Seya T., Atkinson J.P. J. Exp. Med. 168:181-194(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D), PROTEIN SEQUENCE OF 35-58, INTERACTION WITH C3B.
[2]	"Alternatively spliced RNAs encode several isoforms of CD46 (MCP), a regulator of complement activation." Purcell D.F., Russell S.M., Deacon N.J., Brown M.A., Hooker D.J., McKenzie I.F. Immunogenetics 33:335-344(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), ALTERNATIVE SPLICING.
[3]	"Membrane cofactor protein of the complement system: alternative splicing of serine/threonine/proline-rich exons and cytoplasmic tails produces multiple isoforms that correlate with protein phenotype." Post T.W., Liszewski M.K., Adams E.M., Tedja I., Miller E.A., Atkinson J.P. J. Exp. Med. 174:93-102(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B; C; D; E AND F).
[4]	"Characterization of a cDNA clone coding for human testis membrane cofactor protein (MCP, CD46)." Cervoni F., Fenichel P., Akhoundi C., Hsi B.L., Rossi B. Mol. Reprod. Dev. 34:107-113(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM F). Tissue: Testis.
[5]	"Post-translational modification and intracellular localization of a splice product of CD46 cloned from human testis: role of the intracellular domains in O-glycosylation." Hara T., Suzuki Y., Nakazawa T., Nishimura H., Nagasawa S., Nishiguchi M., Matsumoto M., Hatanaka M., Kitamura M., Seya T. Immunology 93:546-555(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM N). Tissue: Testis.
[6]	"Molecular cloning of human CD46 (membrane cofactor protein) CDS from cancer cell lines in a retroviral vector system." Xue Z.T., Widegren B., Salford L. Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS D; F AND L).
[7]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D). Tissue: Teratocarcinoma.
[8]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS D AND E). Tissue: Fetal kidney, Liver and Salivary gland.
[9]	Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B), VARIANT PHE-13. Tissue: Liver.
[10]	SeattleSNPs variation discovery resource Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASN-266; LEU-324; VAL-353 AND GLY-355.
[11]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[13]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D). Tissue: Testis.
[14]	"Analysis of measles virus binding sites of the CD46 gene in patients with subacute sclerosing panencephalitis." Kusuhara K., Sasaki Y., Nakao F., Ihara K., Hattori H., Yamashita S., Nihei K., Koide N., Aiba H., Takeshita K., Hara T. J. Infect. Dis. 181:1447-1449(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-158, VARIANTS PHE-13 AND GLN-59.
[15]	"Characterization of the promoter region of the membrane cofactor protein (CD46) gene of the human complement system and comparison to a membrane cofactor protein-like genetic element." Cui W., Hourcade D., Post T.W., Greenlund A.C., Atkinson J.P., Kumar V. J. Immunol. 151:4137-4146(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
[16]	"Homology of an acrosome-reacted sperm-specific antigen to CD46." Okabe M., Ying X., Nagira M., Ikawa M., Kohama Y., Mimura T., Tanaka K. J. Pharmacobio-Dyn. 15:455-459(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 35-60. Tissue: Sperm.
[17]	"Human non-lineage antigen, CD46 (HuLy-m5): purification and partial sequencing demonstrates structural homology with complement-regulating glycoproteins." Purcell D.F., Deacon N.J., Andrew S.M., McKenzie I.F. Immunogenetics 31:21-28(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 35-58.
[18]	"Human membrane cofactor protein (CD46) acts as a cellular receptor for measles virus." Naniche D., Varior-Krishnan G., Cervoni F., Wild T.F., Rossi B., Rabourdin-Combe C., Gerlier D. J. Virol. 67:6025-6032(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 35-49, BINDING TO MEASLES VIRUS.
[19]	"Contribution of the repeating domains of membrane cofactor protein (CD46) of the complement system to ligand binding and cofactor activity." Adams E.M., Brown M.C., Nunge M., Krych M., Atkinson J.P. J. Immunol. 147:3005-3011(1991) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH C3B AND C4B.
[20]	"Tissue-specific and allelic expression of the complement regulator CD46 is controlled by alternative splicing." Russell S.M., Sparrow R.L., McKenzie I.F.C., Purcell D.F.J. Eur. J. Immunol. 22:1513-1518(1992) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING.
[21]	"The human CD46 molecule is a receptor for measles virus (Edmonston strain)." Doerig R.E., Marcil A., Chopra A., Richardson C.D. Cell 75:295-305(1993) [PubMed] [Europe PMC] [Abstract] Cited for: BINDING TO MEASLES VIRUS.
[22]	"Measles virus and C3 binding sites are distinct on membrane cofactor protein (CD46)." Manchester M., Valsamakis A., Kaufman R., Liszewski M.K., Alvarez J., Atkinson J.P., Lublin D.M., Oldstone M.B. Proc. Natl. Acad. Sci. U.S.A. 92:2303-2307(1995) [PubMed] [Europe PMC] [Abstract] Cited for: BINDING TO MEASLES VIRUS.
[23]	"Membrane cofactor protein (CD46) is a keratinocyte receptor for the M protein of the group A streptococcus." Okada N., Liszewski M.K., Atkinson J.P., Caparon M. Proc. Natl. Acad. Sci. U.S.A. 92:2489-2493(1995) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH STREPTOCOCCUS PYOGENES M PROTEIN.
[24]	"The N-glycan of the SCR 2 region is essential for membrane cofactor protein (CD46) to function as a measles virus receptor." Maisner A., Alvarez J., Liszewski M.K., Atkinson D.J., Atkinson J.P., Herrler G. J. Virol. 70:4973-4977(1996) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF ASN-83; ASN-114 AND ASN-273.
[25]	"Membrane cofactor protein (MCP or CD46) is a cellular pilus receptor for pathogenic Neisseria." Kaellstroem H., Liszewski M.K., Atkinson J.P., Jonsson A.-B. Mol. Microbiol. 25:639-647(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NEISSERIA TYPE IV PILI.
[26]	"Membrane cofactor protein: importance of N- and O-glycosylation for complement regulatory function." Liszewski M.K., Leung M.K., Atkinson J.P. J. Immunol. 161:3711-3718(1998) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF ASN-83; ASN-114 AND ASN-273.
[27]	"CD46 is a cellular receptor for human herpesvirus 6." Santoro F., Kennedy P.E., Locatelli G., Malnati M.S., Berger E.A., Lusso P. Cell 99:817-827(1999) [PubMed] [Europe PMC] [Abstract] Cited for: BINDING OF HUMAN HERPESVIRUS 6.
[28]	"Membrane cofactor protein (MCP; CD46): isoform-specific tyrosine phosphorylation." Wang G., Liszewski M.K., Chan A.C., Atkinson J.P. J. Immunol. 164:1839-1846(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION (ISOFORMS B/D/F/H/J/L/3).
[29]	"CD46, a new costimulatory molecule for T cells, that induces p120CBL and LAT phosphorylation." Astier A., Trescol-Biemont M.-C., Azocar O., Lamouille B., Rabourdin-Combe C. J. Immunol. 164:6091-6095(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[30]	"SLAM (CDw150) is a cellular receptor for measles virus." Tatsuo H., Ono N., Tanaka K., Yanagi Y. Nature 406:893-897(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MEASLES VIRUS H PROTEIN.
[31]	"Attachment of Neisseria gonorrhoeae to the cellular pilus receptor CD46: identification of domains important for bacterial adherence." Kaellstroem H., Blackmer Gill D., Albiger B., Liszewski M.K., Atkinson J.P., Jonsson A.-B. Cell. Microbiol. 3:133-143(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NEISSERIA TYPE IV PILI, MUTAGENESIS OF ASN-83; ASN-114 AND ASN-273.
[32]	"Human Herpesvirus 6 and Measles Virus employ distinct CD46 domains for receptor function." Greenstone H.L., Santoro F., Lusso P., Berger E.A. J. Biol. Chem. 277:39112-39118(2002) [PubMed] [Europe PMC] [Abstract] Cited for: BINDING OF HUMAN HERPESVIRUS 6.
[33]	"CD46 is phosphorylated at tyrosine 354 upon infection of epithelial cells by Neisseria gonorrhoeae." Lee S.W., Bonnah R.A., Higashi D.L., Atkinson J.P., Milgram S.L., So M. J. Cell Biol. 156:951-957(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION (ISOFORMS B/D/F/H/J/L/3).
[34]	"Identification of the streptococcal M protein binding site on membrane cofactor protein (CD46)." Giannakis E., Jokiranta T.S., Ormsby R.J., Duthy T.G., Male D.A., Christiansen D., Fischetti V.A., Bagley C., Loveland B.E., Gordon D.L. J. Immunol. 168:4585-4592(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH STREPTOCOCCUS PYOGENES M PROTEIN.
[35]	"Characterization of human membrane cofactor protein (MCP; CD46) on spermatozoa." Riley R.C., Kemper C., Leung M., Atkinson J.P. Mol. Reprod. Dev. 62:534-546(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION.
[36]	"Interaction of glycoprotein H of human herpesvirus 6 with the cellular receptor CD46." Santoro F., Greenstone H.L., Insinga A., Liszewski M.K., Atkinson J.P., Lusso P., Berger E.A. J. Biol. Chem. 278:25964-25969(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HUMAN HERPESVIRUS 6 GH PROTEIN.
[37]	"Down-regulation of CD46 by piliated Neisseria gonorrhoeae." Gill D.B., Koomey M., Cannon J.G., Atkinson J.P. J. Exp. Med. 198:1313-1322(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[38]	"Human herpesvirus 6 variant A glycoprotein H-glycoprotein L-glycoprotein Q complex associates with human CD46." Mori Y., Yang X., Akkapaiboon P., Okuno T., Yamanishi K. J. Virol. 77:4992-4999(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HUMAN HERPESVIRUS 6 GH PROTEIN.
[39]	"Adenovirus type 11 uses CD46 as a cellular receptor." Segerman A., Atkinson J.P., Marttila M., Dennerquist V., Wadell G., Arnberg N. J. Virol. 77:9183-9191(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HUMAN ADENOVIRUS B TYPE 11 PIV/FIBER PROTEIN.
[40]	"Familial haemolytic uraemic syndrome and an MCP mutation." Noris M., Brioschi S., Caprioli J., Todeschini M., Bresin E., Porrati F., Gamba S., Remuzzi G. Lancet 362:1542-1547(2003) [PubMed] [Europe PMC] [Abstract] Cited for: DISEASE.
[41]	"Activation of human CD4+ cells with CD3 and CD46 induces a T-regulatory cell 1 phenotype." Kemper C., Chan A.C., Green J.M., Brett K.A., Murphy K.M., Atkinson J.P. Nature 421:388-392(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[42]	"CD46 is a cellular receptor for group B adenoviruses." Gaggar A., Shayakhmetov D.M., Lieber A. Nat. Med. 9:1408-1412(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HUMAN ADENOVIRUS B PIV/FIBER PROTEIN, IDENTIFICATION BY MASS SPECTROMETRY.
[43]	"Complement inhibitor membrane cofactor protein (MCP; CD46) is constitutively shed from cancer cell membranes in vesicles and converted by a metalloproteinase to a functionally active soluble form." Hakulinen J., Junnikkala S., Sorsa T., Meri S. Eur. J. Immunol. 34:2620-2629(2004) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION, SUBCELLULAR LOCATION.
[44]	"Membrane cofactor protein is a receptor for adenoviruses associated with epidemic keratoconjunctivitis." Wu E., Trauger S.A., Pache L., Mullen T.-M., von Seggern D.J., Siuzdak G., Nemerow G.R. J. Virol. 78:3897-3905(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HUMAN ADENOVIRUS D TYPE 37 PIV/FIBER PROTEIN, IDENTIFICATION BY MASS SPECTROMETRY.
[45]	"The human membrane cofactor CD46 is a receptor for species B adenovirus serotype 3." Sirena D., Lilienfeld B., Eisenhut M., Kaelin S., Boucke K., Beerli R.R., Vogt L., Ruedl C., Bachmann M.F., Greber U.F., Hemmi S. J. Virol. 78:4454-4462(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HUMAN ADENOVIRUS B TYPE 3 PIV/FIBER PROTEIN.
[46]	"Localization of regions in CD46 that interact with adenovirus." Gaggar A., Shayakhmetov D.M., Liszewski M.K., Atkinson J.P., Lieber A. J. Virol. 79:7503-7513(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HUMAN ADENOVIRUS B TYPE 35 PIV/FIBER PROTEIN.
[47]	"CD46 is a cellular receptor for all species B adenoviruses except types 3 and 7." Marttila M., Persson D., Gustafsson D., Liszewski M.K., Atkinson J.P., Wadell G., Arnberg N. J. Virol. 79:14429-14436(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HUMAN ADENOVIRUS B PIV/FIBER PROTEIN.
[48]	"Crystal structure of two CD46 domains reveals an extended measles virus-binding surface." Casasnovas J.M., Larvie M., Stehle T. EMBO J. 18:2911-2922(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 35-160.
[49]	"Mutations in human complement regulator, membrane cofactor protein (CD46), predispose to development of familial hemolytic uremic syndrome." Richards A., Kemp E.J., Liszewski M.K., Goodship J.A., Lampe A.K., Decorte R., Muesluemanoglu M.H., Kavukcu S., Filler G., Pirson Y., Wen L.S., Atkinson J.P., Goodship T.H.J. Proc. Natl. Acad. Sci. U.S.A. 100:12966-12971(2003) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS AHUS2 PRO-240 AND 271-ASP-SER-272 DEL.
[50]	"Genetics of HUS: the impact of MCP, CFH, and IF mutations on clinical presentation, response to treatment, and outcome." The international registry of recurrent and familial HUS/TTP Caprioli J., Noris M., Brioschi S., Pianetti G., Castelletti F., Bettinaglio P., Mele C., Bresin E., Cassis L., Gamba S., Porrati F., Bucchioni S., Monteferrante G., Fang C.J., Liszewski M.K., Kavanagh D., Atkinson J.P., Remuzzi G. Blood 108:1267-1279(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AHUS2 TYR-35.
[51]	"Insights into hemolytic uremic syndrome: segregation of three independent predisposition factors in a large, multiple affected pedigree." Esparza-Gordillo J., Jorge E.G., Garrido C.A., Carreras L., Lopez-Trascasa M., Sanchez-Corral P., de Cordoba S.R. Mol. Immunol. 43:1769-1775(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AHUS2 SER-165.
[52]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] TYR-228 AND VAL-353.
[53]	"Mutations in alternative pathway complement proteins in American patients with atypical hemolytic uremic syndrome." Maga T.K., Nishimura C.J., Weaver A.E., Frees K.L., Smith R.J.H. Hum. Mutat. 31:E1445-E1460(2010) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS AHUS2 CYS-216 AND ARG-231.
+	Additional computationally mapped references.

Web resources

GeneReviews

SeattleSNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y00651 mRNA. Translation: CAA68675.1.
M58050 mRNA. Translation: AAA62833.1.
X59405 mRNA. No translation available.
X59406 mRNA. No translation available.
X59407 mRNA. No translation available.
X59408 mRNA. No translation available.
X59409 mRNA. No translation available.
X59410 mRNA. No translation available.
S51940 mRNA. Translation: AAB24802.1.
D84105 mRNA. Translation: BAA12224.1.
EF076055 mRNA. Translation: ABK81635.1.
EF076056 mRNA. Translation: ABK81636.1.
EF076057 mRNA. Translation: ABK81637.1.
EF076058 mRNA. Translation: ABK81638.1.
AK291227 mRNA. Translation: BAF83916.1.
BX537451 mRNA. Translation: CAD97694.1.
BX640613 mRNA. Translation: CAE45719.1.
BX649050 mRNA. Translation: CAI45983.1.
AK222822 mRNA. Translation: BAD96542.1.
AY916779 Genomic DNA. Translation: AAW82433.1.
AL365178, AL035209 Genomic DNA. Translation: CAH73947.1.
AL365178, AL035209 Genomic DNA. Translation: CAH73948.1.
AL365178, AL035209 Genomic DNA. Translation: CAH73949.1.
AL365178, AL035209 Genomic DNA. Translation: CAH73950.1.
AL365178, AL035209 Genomic DNA. Translation: CAH73951.1.
AL365178, AL035209 Genomic DNA. Translation: CAH73952.1.
AL365178, AL035209 Genomic DNA. Translation: CAH73953.1.
AL365178, AL035209 Genomic DNA. Translation: CAH73954.1.
AL035209, AL365178 Genomic DNA. Translation: CAI18804.1.
AL035209, AL365178 Genomic DNA. Translation: CAI18805.1.
AL035209, AL365178 Genomic DNA. Translation: CAI18806.1.
AL035209, AL365178 Genomic DNA. Translation: CAI18807.1.
AL035209, AL365178 Genomic DNA. Translation: CAI18808.1.
AL035209, AL365178 Genomic DNA. Translation: CAI18809.1.
AL035209, AL365178 Genomic DNA. Translation: CAI18810.1.
AL035209, AL365178 Genomic DNA. Translation: CAI18811.1.
CH471100 Genomic DNA. Translation: EAW93465.1.
CH471100 Genomic DNA. Translation: EAW93470.1.
CH471100 Genomic DNA. Translation: EAW93476.1.
BC030594 mRNA. Translation: AAH30594.1.
AF209712 mRNA. Translation: AAF73844.1.
AF209713 mRNA. Translation: AAF73845.1.
AF209714 mRNA. Translation: AAF73846.1.
S65879 Genomic DNA. Translation: AAD13968.1.

IPI

IPI00012035.
IPI00173903.
IPI00219852.
IPI00219853.
IPI00332397.
IPI00332399.
IPI00332401.
IPI00337661.
IPI00374175.
IPI00374176.
IPI00374177.
IPI00374178.
IPI00398353.
IPI00398354.
IPI00456644.
IPI00479283.

PIR

G02913.
I54479.
I57998.
S01896.

RefSeq

NP_002380.3. NM_002389.4.
NP_722548.1. NM_153826.3.
NP_758860.1. NM_172350.2.
NP_758861.1. NM_172351.2.
NP_758862.1. NM_172352.2.
NP_758863.1. NM_172353.2.
NP_758869.1. NM_172359.2.
NP_758871.1. NM_172361.2.

UniGene

Hs.510402.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CKL	X-ray	3.10	A/B/C/D/E/F	35-160	[»]
1HR4	model	-	A	159-284	[»]
2O39	X-ray	2.85	C/D	35-160	[»]
3INB	X-ray	3.10	C/D	35-160	[»]
3L89	X-ray	3.50	M/N/O/P/Q/R/S/T/U/V/W/X	35-160	[»]
3O8E	X-ray	2.84	B/D	35-286	[»]

ProteinModelPortal

P15529.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-41232N.

IntAct

P15529. 4 interactions.

MINT

MINT-222279.

PTM databases

PhosphoSite

P15529.

Polymorphism databases

DMDM

41019474.

Proteomic databases

PaxDb

P15529.

PRIDE

P15529.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000322875; ENSP00000313875; ENSG00000117335.
ENST00000322918; ENSP00000314664; ENSG00000117335.
ENST00000354848; ENSP00000346912; ENSG00000117335.
ENST00000357714; ENSP00000350346; ENSG00000117335.
ENST00000358170; ENSP00000350893; ENSG00000117335.
ENST00000360212; ENSP00000353342; ENSG00000117335.
ENST00000361067; ENSP00000354358; ENSG00000117335.
ENST00000367041; ENSP00000356008; ENSG00000117335.
ENST00000367042; ENSP00000356009; ENSG00000117335.
ENST00000367047; ENSP00000356014; ENSG00000117335.
ENST00000441839; ENSP00000413543; ENSG00000117335.
ENST00000480003; ENSP00000418471; ENSG00000117335.

GeneID

4179.

KEGG

hsa:4179.

UCSC

uc001hgc.3. human.
uc001hgg.3. human.
uc001hgh.3. human.
uc001hgi.3. human.
uc001hgj.3. human.
uc001hgl.3. human.
uc001hgm.3. human.
uc001hgp.3. human.

Organism-specific databases

CTD

4179.

GeneCards

GC01P207925.

HGNC

HGNC:6953. CD46.

HPA

CAB010401.
HPA016903.

MIM

120920. gene+phenotype.
612922. phenotype.

neXtProt

NX_P15529.

Orphanet

93576. Atypical hemolytic uremic syndrome with MCP/CD46 anomaly.
244242. HELLP syndrome.

PharmGKB

PA30700.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG151270.

HOVERGEN

HBG006335.

KO

K04007.

OMA

FEYLDAV.

OrthoDB

EOG418BP6.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P15529.

Bgee

P15529.

Genevestigator

P15529.

GermOnline

ENSG00000117335. Homo sapiens.

Family and domain databases

InterPro

IPR017341. M_CF_CD46.
IPR000436. Sushi_SCR_CCP.
[Graphical view]

Pfam

PF00084. Sushi. 4 hits.
[Graphical view]

PIRSF

PIRSF037971. TLX_CD46. 1 hit.

SMART

SM00032. CCP. 4 hits.
[Graphical view]

SUPFAM

SSF57535. Complement_control_module. 4 hits.

PROSITE

PS50923. SUSHI. 4 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

CD46. human.

EvolutionaryTrace

P15529.

GenomeRNAi

4179.

NextBio

16458.

PMAP-CutDB

P15529.

SOURCE

Search...

Entry information

Entry name

MCP_HUMAN

Accession

Primary (citable) accession number: P15529
Secondary accession number(s): A0T1T0 , A0T1T1, A0T1T2, Q15429, Q53GV9, Q5HY94, Q5VWS6, Q5VWS7, Q5VWS8, Q5VWS9, Q5VWT0, Q5VWT1, Q5VWT2, Q6N0A1, Q7Z3R5, Q9NNW2, Q9NNW3, Q9NNW4, Q9UCJ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	January 16, 2004
Last modified:	May 1, 2013
This is version 158 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.