Q9UMF0 (ICAM5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Intercellular adhesion molecule 5
Short name=ICAM-5

Alternative name(s):
Telencephalin

Gene names

Name:	ICAM5
Synonyms:	TLCN, TLN

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	924 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	ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2).
Subcellular location	Membrane; Single-pass type I membrane protein.
Tissue specificity	Expressed on neurons in the most rostral segment of the mammalian brain, the telencephalon.
Sequence similarities	Belongs to the immunoglobulin superfamily. ICAM family. Contains 9 Ig-like C2-type (immunoglobulin-like) domains.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell-cell adhesion Inferred from electronic annotation. Source: InterPro
Cellular component	integral to plasma membrane Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 31

31

Potential

Chain

32 – 924

893

Intercellular adhesion molecule 5

PRO_0000014799

Regions

Topological domain

32 – 835

804

Extracellular Potential

Transmembrane

836 – 856

21

Helical; Potential

Topological domain

857 – 924

68

Cytoplasmic Potential

Domain

48 – 130

83

Ig-like C2-type 1

Domain

135 – 235

101

Ig-like C2-type 2

Domain

242 – 329

88

Ig-like C2-type 3

Domain

337 – 402

66

Ig-like C2-type 4

Domain

408 – 486

79

Ig-like C2-type 5

Domain

491 – 568

78

Ig-like C2-type 6

Domain

573 – 662

90

Ig-like C2-type 7

Domain

666 – 739

74

Ig-like C2-type 8

Domain

746 – 830

85

Ig-like C2-type 9

Amino acid modifications

Modified residue

182

1

Phosphothreonine Ref.4

Modified residue

184

1

Phosphothreonine Ref.4

Glycosylation

54

1

N-linked (GlcNAc...) Ref.5

Glycosylation

74

1

N-linked (GlcNAc...) Ref.5

Glycosylation

137

1

N-linked (GlcNAc...) Ref.5

Glycosylation

195

1

N-linked (GlcNAc...) Ref.5

Glycosylation

214

1

N-linked (GlcNAc...) Ref.5

Glycosylation

303

1

N-linked (GlcNAc...) Potential

Glycosylation

316

1

N-linked (GlcNAc...) Potential

Glycosylation

371

1

N-linked (GlcNAc...) Potential

Glycosylation

397

1

N-linked (GlcNAc...) Potential

Glycosylation

583

1

N-linked (GlcNAc...) Potential

Glycosylation

646

1

N-linked (GlcNAc...) Potential

Glycosylation

764

1

N-linked (GlcNAc...) Potential

Glycosylation

795

1

N-linked (GlcNAc...) Potential

Glycosylation

796

1

N-linked (GlcNAc...) Potential

Disulfide bond

55 ↔ 99

Ref.5

Disulfide bond

59 ↔ 103

Ref.5

Disulfide bond

142 ↔ 198

Ref.5

Disulfide bond

249 ↔ 302

By similarity

Disulfide bond

344 ↔ 383

By similarity

Disulfide bond

415 ↔ 470

By similarity

Disulfide bond

498 ↔ 552

By similarity

Disulfide bond

580 ↔ 645

By similarity

Disulfide bond

673 ↔ 725

By similarity

Disulfide bond

769 ↔ 814

By similarity

Natural variations

Natural variant

140

1

L → V in a breast cancer sample; somatic mutation. Ref.6

VAR_035515

Natural variant

188

1

R → W in a breast cancer sample; somatic mutation. Ref.6

VAR_035516

Natural variant

301

1

V → I. Ref.1
Corresponds to variant rs1056538 [ dbSNP | Ensembl ].

VAR_056046

Natural variant

348

1

A → T. Ref.1
Corresponds to variant rs2228615 [ dbSNP | Ensembl ].

VAR_056047

Natural variant

488

1

E → Q in a breast cancer sample; somatic mutation. Ref.6

VAR_035517

Experimental info

Sequence conflict

614

1

A → T in AAC50959. Ref.1

Sequence conflict

786

1

G → R in AAC97931. Ref.2

Sequence conflict

816

1

A → R in AAC50959. Ref.1

Sequence conflict

816

1

A → R in AAC97931. Ref.2

Secondary structure

1

.

.

.

.

.

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.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

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.

.

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.

.

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.

.

.

.

924

Helix Strand Turn

Details...

Beta strand

36 – 46

11

Beta strand

51 – 57

7

Beta strand

70 – 73

4

Beta strand

82 – 89

8

Beta strand

92 – 95

4

Beta strand

98 – 103

6

Beta strand

106 – 110

5

Beta strand

114 – 117

4

Beta strand

130 – 133

4

Beta strand

137 – 143

7

Helix

150 – 152

3

Beta strand

153 – 158

6

Beta strand

163 – 168

6

Beta strand

180 – 186

7

Helix

189 – 191

3

Beta strand

195 – 202

8

Beta strand

212 – 215

4

Sequences

	Sequence		Length	Mass (Da)
	Q9UMF0 [UniParc]. Last modified May 18, 2010. Version 3. Checksum: 97D0A9467BD16D30	FASTA	924	97,116
	10 20 30 40 50 60 MPGPSPGLRR ALLGLWAALG LGLFGLSAVS QEPFWADLQP RVAFVERGGS LWLNCSTNCP 70 80 90 100 110 120 RPERGGLETS LRRNGTQRGL RWLARQLVDI REPETQPVCF FRCARRTLQA RGLIRTFQRP 130 140 150 160 170 180 DRVELMPLPP WQPVGENFTL SCRVPGAGPR ASLTLTLLRG AQELIRRSFA GEPPRARGAV 190 200 210 220 230 240 LTATVLARRE DHGANFSCRA ELDLRPHGLG LFENSSAPRE LRTFSLSPDA PRLAAPRLLE 250 260 270 280 290 300 VGSERPVSCT LDGLFPASEA RVYLALGDQN LSPDVTLEGD AFVATATATA SAEQEGARQL 310 320 330 340 350 360 VCNVTLGGEN RETRENVTIY SFPAPLLTLS EPSVSEGQMV TVTCAAGAQA LVTLEGVPAA 370 380 390 400 410 420 VPGQPAQLQL NATENDDRRS FFCDATLDVD GETLIKNRSA ELRVLYAPRL DDSDCPRSWT 430 440 450 460 470 480 WPEGPEQTLR CEARGNPEPS VHCARSDGGA VLALGLLGPV TRALSGTYRC KAANDQGEAV 490 500 510 520 530 540 KDVTLTVEYA PALDSVGCPE RITWLEGTEA SLSCVAHGVP PPDVICVRSG ELGAVIEGLL 550 560 570 580 590 600 RVAREHAGTY RCEATNPRGS AAKNVAVTVE YGPRFEEPSC PSNWTWVEGS GRLFSCEVDG 610 620 630 640 650 660 KPQPSVKCVG SGGATEGVLL PLAPPDPSPR APRIPRVLAP GIYVCNATNR HGSVAKTVVV 670 680 690 700 710 720 SAESPPEMDE STCPSHQTWL EGAEASALAC AARGRPSPGV RCSREGIPWP EQQRVSREDA 730 740 750 760 770 780 GTYHCVATNA HGTDSRTVTV GVEYRPVVAE LAASPPGGVR PGGNFTLTCR AEAWPPAQIS 790 800 810 820 830 840 WRAPPGALNI GLSSNNSTLS VAGAMGSHGG EYECAATNAH GRHARRITVR VAGPWLWVAV 850 860 870 880 890 900 GGAAGGAALL AAGAGLAFYV QSTACKKGEY NVQEAESSGE AVCLNGAGGG AGGAAGAEGG 910 920 PEAAGGAAES PAEGEVFAIQ LTSA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning and chromosomal localization of the human telencephalin and its distinctive interaction with lymphocyte function-associated antigen-1." Mizuno T., Yoshihara Y., Inazawa J., Kagamiyama H., Mori K. J. Biol. Chem. 272:1156-1163(1997) [PubMed: 8995416] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ILE-301 AND THR-348. Tissue: Brain.
[2]	"Mapping of the ICAM-5 (telencephalin) gene, a neuronal member of the ICAM family, to a location between ICAM-1 and ICAM-3 on human chromosome 19p13.2." Kilgannon P., Turner T., Meyer J., Wisdom W., Gallatin W.M. Genomics 54:328-330(1998) [PubMed: 9828136] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The DNA sequence and biology of human chromosome 19." Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M. Nature 428:529-535(2004) [PubMed: 15057824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry." Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C. Anal. Chem. 76:2763-2772(2004) [PubMed: 15144186] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-182 AND THR-184, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[5]	"An unusual allosteric mobility of the C-terminal helix of a high-affinity alphaL integrin I domain variant bound to ICAM-5." Zhang H., Casasnovas J.M., Jin M., Liu J.H., Gahmberg C.G., Springer T.A., Wang J.H. Mol. Cell 31:432-437(2008) [PubMed: 18691975] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 32-227 IN COMPLEX WITH ITGAL, GLYCOSYLATION AT ASN-54; ASN-74; ASN-137; ASN-195 AND ASN-214, DISULFIDE BONDS.
[6]	"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: 16959974] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-140; TRP-188 AND GLN-488.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U72671 mRNA. Translation: AAC50959.1.
AF082802 Genomic DNA. Translation: AAC97931.1.
AC011511 Genomic DNA. No translation available.

IPI

IPI00290456.

RefSeq

NP_003250.3. NM_003259.3.

UniGene

Hs.465862.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3BN3	X-ray	2.10	B	32-227	[»]

ProteinModelPortal

Q9UMF0.

SMR

Q9UMF0. Positions 32-839.

ModBase

Search...

Protein-protein interaction databases

STRING

Q9UMF0.

PTM databases

PhosphoSite

Q9UMF0.

Polymorphism databases

DMDM

296439327.

Proteomic databases

PRIDE

Q9UMF0.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000221980; ENSP00000221980; ENSG00000105376.

GeneID

7087.

KEGG

hsa:7087.

Organism-specific databases

CTD

7087.

GeneCards

GC19P010400.

HGNC

HGNC:5348. ICAM5.

HPA

CAB025178.
HPA008943.
HPA009083.

MIM

601852. gene.

neXtProt

NX_Q9UMF0.

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00530000063246.

HOGENOM

HBG127163.

HOVERGEN

HBG052077.

InParanoid

Q9UMF0.

OMA

SVHCARP.

OrthoDB

EOG4HMJ8M.

PhylomeDB

Q9UMF0.

Gene expression databases

ArrayExpress

Q9UMF0.

Bgee

Q9UMF0.

CleanEx

HS_ICAM5.

Genevestigator

Q9UMF0.

GermOnline

ENSG00000105376. Homo sapiens.

Family and domain databases

InterPro

IPR003988. ICAM.
IPR013768. ICAM_N.
IPR003987. ICAM_VCAM_N.
IPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
[Graphical view]

Gene3D

G3DSA:2.60.40.10. Ig-like_fold. 12 hits.

KO

K06769.

Pfam

PF07679. I-set. 1 hit.
PF03921. ICAM_N. 1 hit.
[Graphical view]

PRINTS

PR01473. ICAM.
PR01472. ICAMVCAM1.

SMART

SM00409. IG. 4 hits.
SM00408. IGc2. 1 hit.
[Graphical view]

PROSITE

PS50835. IG_LIKE. 4 hits.
[Graphical view]

ProtoNet

Search...

Other

SOURCE

Search...

Entry information

Entry name

ICAM5_HUMAN

Accession

Primary (citable) accession number: Q9UMF0
Secondary accession number(s): Q9Y6F3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 18, 2001
Last sequence update:	May 18, 2010
Last modified:	January 25, 2012
This is version 104 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.