P22897 (MRC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Macrophage mannose receptor 1
Short name=MMR

Alternative name(s):
C-type lectin domain family 13 member D
C-type lectin domain family 13 member D-like
Macrophage mannose receptor 1-like protein 1
CD_antigen=CD206

Gene names

Name:	MRC1
Synonyms:	CLEC13D, CLEC13DL, MRC1L1

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	1456 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	Mediates the endocytosis of glycoproteins by macrophages. Binds both sulfated and non-sulfated polysaccharide chains. Acts as phagocytic receptor for bacteria, fungi and other pathogens.
Subcellular location	Endosome membrane; Single-pass type I membrane protein. Cell membrane; Single-pass type I membrane protein Ref.10.
Polymorphism	Genetic variations in MRC1 may influence susceptibility or resistance to leprosy in some populations. Particularly, Gly-396 seems to be a risk factor for leprosy when associated with Ala-399 and Phe-407.
Miscellaneous	CRDs 1-3 have at most very weak affinity for carbohydrate. CRD 4 shows the highest affinity binding and has multispecificity for a variety of monosaccharides. At least 3 CRDs (4, 5, and 7) are required for high affinity binding and endocytosis of multivalent glycoconjugates.
Sequence similarities	Contains 8 C-type lectin domains. Contains 1 fibronectin type-II domain. Contains 1 ricin B-type lectin domain.
Sequence caution	The sequence CAH70733.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAH70872.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAH71176.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAI15339.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Endocytosis
Cellular component	Cell membrane Endosome Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Signal Transmembrane Transmembrane helix
Ligand	Calcium Lectin
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	receptor-mediated endocytosis Inferred from direct assay Ref.10. Source: UniProtKB
Cellular_component	endosome membrane Inferred from direct assay Ref.10. Source: UniProtKB integral to plasma membrane Traceable author statement Ref.3. Source: ProtInc
Molecular_function	mannose binding Traceable author statement Ref.1. Source: ProtInc receptor activity Inferred from direct assay Ref.10. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P22897-1)

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 2 (identifier: P22897-2)

The sequence of this isoform differs from the canonical sequence as follows:
     470-498: DGYWADRGCEWPLGYICKMKSRSQGPEIV → AGVQWHNLGSMQPLPREFKRFSCLSLPSS
     499-1456: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

18

Potential

Chain

19 – 1456

1438

Macrophage mannose receptor 1

PRO_0000017548

Regions

Topological domain

19 – 1389

1371

Extracellular Potential

Transmembrane

1390 – 1410

21

Helical; Potential

Topological domain

1411 – 1456

46

Cytoplasmic Potential

Domain

22 – 142

121

Ricin B-type lectin

Domain

163 – 211

49

Fibronectin type-II

Domain

225 – 341

117

C-type lectin 1

Domain

369 – 487

119

C-type lectin 2

Domain

511 – 626

116

C-type lectin 3

Domain

655 – 778

124

C-type lectin 4

Domain

807 – 923

117

C-type lectin 5

Domain

952 – 1080

129

C-type lectin 6

Domain

1102 – 1213

112

C-type lectin 7

Domain

1241 – 1356

116

C-type lectin 8

Amino acid modifications

Glycosylation

104

1

N-linked (GlcNAc...) Potential

Glycosylation

344

1

N-linked (GlcNAc...) Potential

Glycosylation

529

1

N-linked (GlcNAc...) Potential

Glycosylation

926

1

N-linked (GlcNAc...) Potential

Glycosylation

930

1

N-linked (GlcNAc...) Potential

Glycosylation

1160

1

N-linked (GlcNAc...) Potential

Glycosylation

1205

1

N-linked (GlcNAc...) Ref.8

Glycosylation

1311

1

N-linked (GlcNAc...) Potential

Disulfide bond

35 ↔ 49

By similarity

Disulfide bond

74 ↔ 91

By similarity

Disulfide bond

168 ↔ 194

By similarity

Disulfide bond

182 ↔ 209

By similarity

Disulfide bond

247 ↔ 340

By similarity

Disulfide bond

316 ↔ 332

By similarity

Disulfide bond

391 ↔ 486

By similarity

Disulfide bond

463 ↔ 478

By similarity

Disulfide bond

532 ↔ 625

By similarity

Disulfide bond

600 ↔ 617

By similarity

Disulfide bond

646 ↔ 659

Disulfide bond

680 ↔ 777

Disulfide bond

753 ↔ 769

Disulfide bond

828 ↔ 922

By similarity

Disulfide bond

899 ↔ 914

By similarity

Disulfide bond

977 ↔ 1079

By similarity

Disulfide bond

1052 ↔ 1071

By similarity

Disulfide bond

1123 ↔ 1212

By similarity

Disulfide bond

1190 ↔ 1204

By similarity

Disulfide bond

1263 ↔ 1355

By similarity

Disulfide bond

1332 ↔ 1347

By similarity

Natural variations

Alternative sequence

470 – 498

29

DGYWA…GPEIV → AGVQWHNLGSMQPLPREFKR FSCLSLPSS in isoform 2.

VSP_041340

Alternative sequence

499 – 1456

958

Missing in isoform 2.

VSP_041341

Natural variant

167

1

T → I. Ref.10
Corresponds to variant rs2296414 [ dbSNP | Ensembl ].

VAR_019700

Natural variant

396

1

G → S Probably protective against leprosy when associated with A-399 and F-407. Ref.6 Ref.10
Corresponds to variant rs1926736 [ dbSNP | Ensembl ].

VAR_065250

Natural variant

399

1

T → A. Ref.6 Ref.10
Corresponds to variant rs35950447 [ dbSNP | Ensembl ].

VAR_065251

Natural variant

407

1

L → F. Ref.6 Ref.10
Corresponds to variant rs2437257 [ dbSNP | Ensembl ].

VAR_065252

Experimental info

Sequence conflict

1334

1

A → T in X55635. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1456

Helix Strand Turn

Details...

Beta strand

654 – 657

4

Beta strand

659 – 663

5

Helix

667 – 669

3

Helix

673 – 681

9

Turn

682 – 684

3

Beta strand

685 – 687

3

Helix

693 – 706

14

Beta strand

712 – 718

7

Helix

746 – 748

3

Beta strand

752 – 757

6

Beta strand

764 – 768

5

Beta strand

773 – 778

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 1, 1991. Version 1. Checksum: 264E5AF3C576A5E3	FASTA	1,456	166,012
	10 20 30 40 50 60 MRLPLLLVFA SVIPGAVLLL DTRQFLIYNE DHKRCVDAVS PSAVQTAACN QDAESQKFRW 70 80 90 100 110 120 VSESQIMSVA FKLCLGVPSK TDWVAITLYA CDSKSEFQKW ECKNDTLLGI KGEDLFFNYG 130 140 150 160 170 180 NRQEKNIMLY KGSGLWSRWK IYGTTDNLCS RGYEAMYTLL GNANGATCAF PFKFENKWYA 190 200 210 220 230 240 DCTSAGRSDG WLWCGTTTDY DTDKLFGYCP LKFEGSESLW NKDPLTSVSY QINSKSALTW 250 260 270 280 290 300 HQARKSCQQQ NAELLSITEI HEQTYLTGLT SSLTSGLWIG LNSLSFNSGW QWSDRSPFRY 310 320 330 340 350 360 LNWLPGSPSA EPGKSCVSLN PGKNAKWENL ECVQKLGYIC KKGNTTLNSF VIPSESDVPT 370 380 390 400 410 420 HCPSQWWPYA GHCYKIHRDE KKIQRDALTT CRKEGGDLTS IHTIEELDFI ISQLGYEPND 430 440 450 460 470 480 ELWIGLNDIK IQMYFEWSDG TPVTFTKWLR GEPSHENNRQ EDCVVMKGKD GYWADRGCEW 490 500 510 520 530 540 PLGYICKMKS RSQGPEIVEV EKGCRKGWKK HHFYCYMIGH TLSTFAEANQ TCNNENAYLT 550 560 570 580 590 600 TIEDRYEQAF LTSFVGLRPE KYFWTGLSDI QTKGTFQWTI EEEVRFTHWN SDMPGRKPGC 610 620 630 640 650 660 VAMRTGIAGG LWDVLKCDEK AKFVCKHWAE GVTHPPKPTT TPEPKCPEDW GASSRTSLCF 670 680 690 700 710 720 KLYAKGKHEK KTWFESRDFC RALGGDLASI NNKEEQQTIW RLITASGSYH KLFWLGLTYG 730 740 750 760 770 780 SPSEGFTWSD GSPVSYENWA YGEPNNYQNV EYCGELKGDP TMSWNDINCE HLNNWICQIQ 790 800 810 820 830 840 KGQTPKPEPT PAPQDNPPVT EDGWVIYKDY QYYFSKEKET MDNARAFCKR NFGDLVSIQS 850 860 870 880 890 900 ESEKKFLWKY VNRNDAQSAY FIGLLISLDK KFAWMDGSKV DYVSWATGEP NFANEDENCV 910 920 930 940 950 960 TMYSNSGFWN DINCGYPNAF ICQRHNSSIN ATTVMPTMPS VPSGCKEGWN FYSNKCFKIF 970 980 990 1000 1010 1020 GFMEEERKNW QEARKACIGF GGNLVSIQNE KEQAFLTYHM KDSTFSAWTG LNDVNSEHTF 1030 1040 1050 1060 1070 1080 LWTDGRGVHY TNWGKGYPGG RRSSLSYEDA DCVVIIGGAS NEAGKWMDDT CDSKRGYICQ 1090 1100 1110 1120 1130 1140 TRSDPSLTNP PATIQTDGFV KYGKSSYSLM RQKFQWHEAE TYCKLHNSLI ASILDPYSNA 1150 1160 1170 1180 1190 1200 FAWLQMETSN ERVWIALNSN LTDNQYTWTD KWRVRYTNWA ADEPKLKSAC VYLDLDGYWK 1210 1220 1230 1240 1250 1260 TAHCNESFYF LCKRSDEIPA TEPPQLPGRC PESDHTAWIP FHGHCYYIES SYTRNWGQAS 1270 1280 1290 1300 1310 1320 LECLRMGSSL VSIESAAESS FLSYRVEPLK SKTNFWIGLF RNVEGTWLWI NNSPVSFVNW 1330 1340 1350 1360 1370 1380 NTGDPSGERN DCVALHASSG FWSNIHCSSY KGYICKRPKI IDAKPTHELL TTKADTRKMD 1390 1400 1410 1420 1430 1440 PSKPSSNVAG VVIIVILLIL TGAGLAAYFF YKKRRVHLPQ EGAFENTLYF NSQSSPGTSD 1450 MKDLVGNIEQ NEHSVI
	Isoform 2 [UniParc]. Checksum: 1305DE544A35A7F4	FASTA	498	56,554
	10 20 30 40 50 60 MRLPLLLVFA SVIPGAVLLL DTRQFLIYNE DHKRCVDAVS PSAVQTAACN QDAESQKFRW 70 80 90 100 110 120 VSESQIMSVA FKLCLGVPSK TDWVAITLYA CDSKSEFQKW ECKNDTLLGI KGEDLFFNYG 130 140 150 160 170 180 NRQEKNIMLY KGSGLWSRWK IYGTTDNLCS RGYEAMYTLL GNANGATCAF PFKFENKWYA 190 200 210 220 230 240 DCTSAGRSDG WLWCGTTTDY DTDKLFGYCP LKFEGSESLW NKDPLTSVSY QINSKSALTW 250 260 270 280 290 300 HQARKSCQQQ NAELLSITEI HEQTYLTGLT SSLTSGLWIG LNSLSFNSGW QWSDRSPFRY 310 320 330 340 350 360 LNWLPGSPSA EPGKSCVSLN PGKNAKWENL ECVQKLGYIC KKGNTTLNSF VIPSESDVPT 370 380 390 400 410 420 HCPSQWWPYA GHCYKIHRDE KKIQRDALTT CRKEGGDLTS IHTIEELDFI ISQLGYEPND 430 440 450 460 470 480 ELWIGLNDIK IQMYFEWSDG TPVTFTKWLR GEPSHENNRQ EDCVVMKGKA GVQWHNLGSM 490 QPLPREFKRF SCLSLPSS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure of the mannose receptor contains multiple motifs resembling carbohydrate-recognition domains." Taylor M.E., Conary J.T., Lennartz M.R., Stahl P.D., Drickamer K. J. Biol. Chem. 265:12156-12162(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE. Tissue: Placenta.
[2]	"Molecular characterization of the human macrophage mannose receptor: demonstration of multiple carbohydrate recognition-like domains and phagocytosis of yeasts in Cos-1 cells." Ezekowitz R.A., Sastry K., Bailly P., Warner A. J. Exp. Med. 172:1785-1794(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"Organization of the gene encoding the human macrophage mannose receptor (MRC1)." Kim S.J., Ruiz N., Bezouska K., Drickamer K. Genomics 14:721-727(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	NHLBI resequencing and genotyping service (RS&G) Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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 2), VARIANTS SER-396; ALA-399 AND PHE-407.
[7]	"Contribution to ligand binding by multiple carbohydrate-recognition domains in the macrophage mannose receptor." Taylor M.E., Bezouska K., Drickamer K. J. Biol. Chem. 267:1719-1726(1992) [PubMed] [Europe PMC] [Abstract] Cited for: STUDIES ON THE BINDING OF INDIVIDUAL LECTIN DOMAINS.
[8]	"Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry." Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F. Proteomics 8:3833-3847(2008) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1205, MASS SPECTROMETRY. Tissue: Milk.
[9]	"Structure of a C-type carbohydrate recognition domain from the macrophage mannose receptor." Feinberg H., Park-Snyder S., Kolatkar A.R., Heise C.T., Taylor M.E., Weis W.I. J. Biol. Chem. 275:21539-21548(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 642-788.
[10]	"Genetic and functional analysis of common MRC1 exon 7 polymorphisms in leprosy susceptibility." Alter A., de Leseleuc L., Van Thuc N., Thai V.H., Huong N.T., Ba N.N., Cardoso C.C., Grant A.V., Abel L., Moraes M.O., Alcais A., Schurr E. Hum. Genet. 127:337-348(2010) [PubMed] [Europe PMC] [Abstract] Cited for: POLYMORPHISM, POSSIBLE ASSOCIATION OF VARIANT SER-396 WITH RESISTANCE TO LEPROSY, VARIANTS ILE-167; ALA-399 AND PHE-407, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - Glycan Binding

Macrophage mannose receptor

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J05550 mRNA. Translation: AAA59868.1.
X55635 mRNA. No translation available.
M93221 , M93192, M93193, M93194, M93195, M93196, M93197, M93198, M93199, M93200, M93201, M93202, M93203, M93204, M93205, M93206, M93207, M93208, M93209, M93210, M93211, M93212, M93213, M93214, M93215, M93216, M93217, M93218, M93219, M93220 Genomic DNA. Translation: AAA60389.1.
EF444997 Genomic DNA. Translation: ACA06020.1.
AL928729, AC069023 Genomic DNA. Translation: CAH70733.1. Sequence problems.
AL139238, AL928580, BX255924 Genomic DNA. Translation: CAH70872.1. Sequence problems.
AL928580, AL139238, BX255924 Genomic DNA. Translation: CAH71176.1. Sequence problems.
BX255924, AL139238, AL928580 Genomic DNA. Translation: CAI15339.1. Sequence problems.
BC142642 mRNA. Translation: AAI42643.1.

IPI

IPI00027848.
IPI00890809.

PIR

A36563.

RefSeq

NP_002429.1. NM_002438.2.
XP_003959976.1. XM_003959927.1.

UniGene

Hs.461247.
Hs.75182.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EGG	X-ray	2.30	A/B	644-787	[»]
1EGI	X-ray	2.30	A/B	644-787	[»]

ProteinModelPortal

P22897.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-101N.

IntAct

P22897. 2 interactions.

STRING

9606.ENSP00000239761.

PTM databases

PhosphoSite

P22897.

Polymorphism databases

DMDM

74746800.

Proteomic databases

PaxDb

P22897.

PRIDE

P22897.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000239761; ENSP00000239761; ENSG00000120586.
ENST00000569591; ENSP00000455897; ENSG00000260314.

GeneID

101060092.
4360.

KEGG

hsa:101060092.
hsa:4360.

UCSC

uc001ipk.3. human.

Organism-specific databases

CTD

4360.

GeneCards

GC10P017852.
GC10P018098.

H-InvDB

HIX0035369.

HGNC

HGNC:7228. MRC1.

HPA

HPA004114.

MIM

153618. gene.

neXtProt

NX_P22897.

PharmGKB

PA134941260.
PA30933.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG288621.

HOGENOM

HOG000113647.

HOVERGEN

HBG107130.

InParanoid

Q5VSK2.

KO

K06560.

OMA

LPCPDGW.

OrthoDB

EOG470TGF.

PhylomeDB

P22897.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P22897.

Bgee

P22897.

CleanEx

HS_MRC1.

Genevestigator

P22897.

Family and domain databases

Gene3D

2.10.10.10. 1 hit.
3.10.100.10. 8 hits.

InterPro

IPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
IPR000562. FN_type2_col-bd.
IPR013806. Kringle-like.
IPR000772. Ricin_B_lectin.
[Graphical view]

Pfam

PF00040. fn2. 1 hit.
PF00059. Lectin_C. 8 hits.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]

SMART

SM00034. CLECT. 8 hits.
SM00059. FN2. 1 hit.
SM00458. RICIN. 1 hit.
[Graphical view]

SUPFAM

SSF56436. C-type_lectin_fold. 8 hits.
SSF57440. Kringle-like. 1 hit.
SSF50370. RicinB_like. 1 hit.

PROSITE

PS00615. C_TYPE_LECTIN_1. 6 hits.
PS50041. C_TYPE_LECTIN_2. 8 hits.
PS00023. FN2_1. 1 hit.
PS51092. FN2_2. 1 hit.
PS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P22897.

NextBio

17159.

SOURCE

Search...

Entry information

Entry name

MRC1_HUMAN

Accession

Primary (citable) accession number: P22897
Secondary accession number(s): A5PKW3, Q5VSJ2, Q5VSK2

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	May 1, 2013
This is version 154 of the entry and version 1 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.