T-cell surface glycoprotein CD5 precursor

Names and origin

Protein names

Recommended name:
    T-cell surface glycoprotein CD5
Alternative name(s):
    Lymphocyte antigen T1/Leu-1
    CD_antigen=CD5

Gene names

Name:	CD5
Synonyms:	LEU1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	495 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	May act as a receptor in regulating T-cell proliferation. CD5 interacts with CD72/LYB-2.
Subcellular location	Membrane; Single-pass type I membrane protein.
Sequence similarities	Contains 3 SRCR domains.

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Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	Repeat Signal Transmembrane
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cell proliferation Ref.1 Non-traceable author statement. Source: UniProtKB cell recognition Ref.7 Non-traceable author statement. Source: UniProtKB
Cellular component	integral to plasma membrane Ref.7 Non-traceable author statement. Source: UniProtKB
Molecular function	scavenger receptor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

24

Chain

25 – 495

471

T-cell surface glycoprotein CD5

PRO_0000033222

Regions

Topological domain

25 – 372

348

Extracellular Potential

Transmembrane

373 – 402

30

Potential

Topological domain

403 – 495

93

Cytoplasmic Potential

Domain

35 – 133

99

SRCR 1

Domain

159 – 268

110

SRCR 2

Domain

276 – 368

93

SRCR 3

Amino acid modifications

Modified residue

439

1

Phosphoserine Ref.8

Modified residue

453

1

Phosphotyrosine Ref.8

Modified residue

460

1

Phosphoserine Ref.8

Modified residue

482

1

Phosphoserine

Modified residue

483

1

Phosphoserine

Modified residue

485

1

Phosphoserine

Glycosylation

116

1

N-linked (GlcNAc...) Potential

Glycosylation

241

1

N-linked (GlcNAc...) Potential

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

By similarity

Disulfide bond

244 ↔ 250

By similarity

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Natural variations

Natural variant

224

1

P → L: dbSNP rs2241002. Ref.4

VAR_020411

Natural variant

461

1

R → H: dbSNP rs637186. Ref.5

VAR_024649

Natural variant

471

1

V → A: dbSNP rs2229177. Ref.5

VAR_058203

Experimental info

Sequence conflict

289

1

V → E in BAF85387. Ref.4

Secondary structure

1

.

495

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P06127-1 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: 8740DD7623DEE1D3
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FASTA

495

54,625

        10         20         30         40         50         60 
MPMGSLQPLA TLYLLGMLVA SCLGRLSWYD PDFQARLTRS NSKCQGQLEV YLKDGWHMVC 

        70         80         90        100        110        120 
SQSWGRSSKQ WEDPSQASKV CQRLNCGVPL SLGPFLVTYT PQSSIICYGQ LGSFSNCSHS 

       130        140        150        160        170        180 
RNDMCHSLGL TCLEPQKTTP PTTRPPPTTT PEPTAPPRLQ LVAQSGGQHC AGVVEFYSGS 

       190        200        210        220        230        240 
LGGTISYEAQ DKTQDLENFL CNNLQCGSFL KHLPETEAGR AQDPGEPREH QPLPIQWKIQ 

       250        260        270        280        290        300 
NSSCTSLEHC FRKIKPQKSG RVLALLCSGF QPKVQSRLVG GSSICEGTVE VRQGAQWAAL 

       310        320        330        340        350        360 
CDSSSARSSL RWEEVCREQQ CGSVNSYRVL DAGDPTSRGL FCPHQKLSQC HELWERNSYC 

       370        380        390        400        410        420 
KKVFVTCQDP NPAGLAAGTV ASIILALVLL VVLLVVCGPL AYKKLVKKFR QKKQRQWIGP 

       430        440        450        460        470        480 
TGMNQNMSFH RNHTATVRSH AENPTASHVD NEYSQPPRNS RLSAYPALEG VLHRSSMQPD 

       490 
NSSDSDYDLH GAQRL

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation of complementary DNA clones encoding the human lymphocyte glycoprotein T1/Leu-1." Jones N.H., Clabby M.L., Dialynas D.P., Huag H.-J.S., Herzenberg L.A., Strominger J.L. Nature 323:346-349(1986) [PubMed: 3093892] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Evolutionarily conserved transcription regulatory elements within the 5'-flanking region of the human CD5 gene." Calvo J., Sole J., Simarro M., Vives J., Lozano F. Tissue Antigens 47:257-261(1996) [PubMed: 8740779] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Lymphocyte.
[3]	Livingston R.J., Shaffer T., McFarland I., Nguyen C.P., Stanaway I.B., Rajkumar N., Johnson E.J., da Ponte S.H., Willa H., Ahearn M.O., Bertucci C., Acklestad J., Carroll A., Swanson J., Gildersleeve H.I., Nickerson D.A. Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"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. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT LEU-224. Tissue: Thymus.
[5]	"Human chromosome 11 DNA sequence and analysis including novel gene identification." Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. Sakaki Y. Nature 440:497-500(2006) [PubMed: 16554811] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS HIS-461 AND ALA-471.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Pancreas.
[7]	"The B-cell surface protein CD72/Lyb-2 is the ligand for CD5." van de Velde H., von Hoegen I., Luo W., Parnes J.R., Thielemans K. Nature 351:662-665(1991) [PubMed: 1711157] [Abstract] Cited for: INTERACTION WITH CD72/LYB-2.
[8]	"Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry." Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T., Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C. Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003) [PubMed: 12522270] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439; TYR-453 AND SER-460, MASS SPECTROMETRY.
[9]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439; TYR-453; SER-482; SER-483 AND SER-485, MASS SPECTROMETRY. Tissue: T-cell.
[10]	"Crystal structure of the third extracellular domain of CD5 reveals the fold of a group B scavenger cysteine-rich receptor domain." Rodamilans B., Munoz I.G., Bragado-Nilsson E., Sarrias M.R., Padilla O., Blanco F.J., Lozano F., Montoya G. J. Biol. Chem. 282:12669-12677(2007) [PubMed: 17322294] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 270-369.
[11]	"Three-dimensional solution structure and conformational plasticity of the N-terminal scavenger receptor cysteine-rich domain of human CD5." Garza-Garcia A., Esposito D., Rieping W., Harris R., Briggs C., Brown M.H., Driscoll P.C. J. Mol. Biol. 378:129-144(2008) [PubMed: 18339402] [Abstract] Cited for: STRUCTURE BY NMR OF 25-134, DISULFIDE BONDS.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

X04391 mRNA. Translation: CAA27979.1.
X89405

AJ237932 Genomic DNA. Translation: CAA61584.2.
EF064752 Genomic DNA. Translation: ABK41935.1.
AK292698 mRNA. Translation: BAF85387.1.
AP000437 Genomic DNA. No translation available.
BC027901 mRNA. Translation: AAH27901.1.

IPI

IPI00025383.

PIR

A26396.

RefSeq

NP_055022.2.

UniGene

Hs.58685

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2JA4	X-ray	2.21	A	270-369	[»]
2JOP	NMR	-	A	25-134	[»]
2JP0	NMR	-	A	25-134	[»]
2OTT	X-ray	2.50	X/Y	276-369	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:21N.

IntAct

P06127. 1 interaction.

STRING

P06127.

PTM databases

GlycoSuiteDB

P06127.

PhosphoSite

P06127.

Proteomic databases

PRIDE

P06127.

Genome annotation databases

Ensembl

ENST00000347785; ENSP00000342681; ENSG00000110448; Homo sapiens. [Genome view]

GeneID

921.

KEGG

hsa:921.

Organism-specific databases

CTD

921.

GeneCards

GC11P060626.

H-InvDB

HIX0009680.

HGNC

HGNC:1685. CD5.

HPA

CAB015392.
CAB020308.

MIM

153340. gene.

PharmGKB

PA26224.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P06127.

HOVERGEN

P06127.

Gene expression databases

ArrayExpress

P06127.

Bgee

P06127.

CleanEx

HS_CD5.

Genevestigator

P06127.

GermOnline

ENSG00000110448. Homo sapiens.

Family and domain databases

InterPro

IPR001190. Srcr_rcpt.
IPR017448. Srcr_rcpt-rel.
IPR003566. Tcell_CD5.
[Graphical view]

PANTHER

PTHR19331:SF6. Tcell_CD5. 1 hit.

Pfam

PF00530. SRCR. 3 hits.
[Graphical view]

PRINTS

PR00258. SPERACTRCPTR.
PR01409. TCELLCD5.

SMART

SM00202. SR. 2 hits.
[Graphical view]

PROSITE

PS00420. SRCR_1. False negative.
PS50287. SRCR_2. 3 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

3810.

SOURCE

Search...

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Entry information

Entry name

CD5_HUMAN

Accession

Primary (citable) accession number: P06127
Secondary accession number(s): A0N0P4, A8K9I3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 1, 1988
Last modified:	November 24, 2009
This is version 106 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.

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