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T-cell surface glycoprotein CD5 (Lymphocyte antigen T1/Leu-1) (CD antigen CD5)

 CD5_HUMAN               Reviewed;         495 AA.
P06127; A0N0P4; A8K9I3;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
30-NOV-2010, sequence version 2.
12-SEP-2018, entry version 181.
RecName: Full=T-cell surface glycoprotein CD5;
AltName: Full=Lymphocyte antigen T1/Leu-1;
AltName: CD_antigen=CD5;
Flags: Precursor;
Name=CD5; Synonyms=LEU1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ARG-461 AND VAL-471.
PubMed=3093892; DOI=10.1038/323346a0;
Jones N.H., Clabby M.L., Dialynas D.P., Huag H.-J.S., Herzenberg L.A.,
Strominger J.L.;
"Isolation of complementary DNA clones encoding the human lymphocyte
glycoprotein T1/Leu-1.";
Nature 323:346-349(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-461 AND VAL-471.
TISSUE=Lymphocyte;
PubMed=8740779; DOI=10.1111/j.1399-0039.1996.tb02551.x;
Calvo J., Sole J., Simarro M., Vives J., Lozano F.;
"Evolutionarily conserved transcription regulatory elements within the
5'-flanking region of the human CD5 gene.";
Tissue Antigens 47:257-261(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-461 AND VAL-471.
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.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LEU-224 AND
ARG-461.
TISSUE=Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
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., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-461 AND
VAL-471.
TISSUE=Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
INTERACTION WITH CD72/LYB-2.
PubMed=1711157; DOI=10.1038/351662a0;
van de Velde H., von Hoegen I., Luo W., Parnes J.R., Thielemans K.;
"The B-cell surface protein CD72/Lyb-2 is the ligand for CD5.";
Nature 351:662-665(1991).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439 AND SER-460, VARIANT
[LARGE SCALE ANALYSIS] ARG-461, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=12522270; DOI=10.1073/pnas.2436191100;
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.;
"Profiling of tyrosine phosphorylation pathways in human cells using
mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-453; SER-483 AND
SER-485, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[11]
X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 270-369.
PubMed=17322294; DOI=10.1074/jbc.M611699200;
Rodamilans B., Munoz I.G., Bragado-Nilsson E., Sarrias M.R.,
Padilla O., Blanco F.J., Lozano F., Montoya G.;
"Crystal structure of the third extracellular domain of CD5 reveals
the fold of a group B scavenger cysteine-rich receptor domain.";
J. Biol. Chem. 282:12669-12677(2007).
[12]
STRUCTURE BY NMR OF 25-134, AND DISULFIDE BONDS.
PubMed=18339402; DOI=10.1016/j.jmb.2008.02.006;
Garza-Garcia A., Esposito D., Rieping W., Harris R., Briggs C.,
Brown M.H., Driscoll P.C.;
"Three-dimensional solution structure and conformational plasticity of
the N-terminal scavenger receptor cysteine-rich domain of human CD5.";
J. Mol. Biol. 378:129-144(2008).
-!- FUNCTION: May act as a receptor in regulating T-cell
proliferation.
-!- SUBUNIT: Interacts with CD72/LYB-2. Interacts with PTPN6/SHP-1 (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein.
-!- PTM: Phosphorylated on tyrosine residues by LYN; this creates
binding sites for PTPN6/SHP-1. {ECO:0000250}.
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EMBL; X04391; CAA27979.1; -; mRNA.
EMBL; X89405; CAA61584.2; -; Genomic_DNA.
EMBL; AJ237927; CAA61584.2; JOINED; Genomic_DNA.
EMBL; AJ237928; CAA61584.2; JOINED; Genomic_DNA.
EMBL; AJ237929; CAA61584.2; JOINED; Genomic_DNA.
EMBL; AJ237930; CAA61584.2; JOINED; Genomic_DNA.
EMBL; AJ237931; CAA61584.2; JOINED; Genomic_DNA.
EMBL; AJ237932; CAA61584.2; JOINED; Genomic_DNA.
EMBL; EF064752; ABK41935.1; -; Genomic_DNA.
EMBL; AK292698; BAF85387.1; -; mRNA.
EMBL; AP000437; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC027901; AAH27901.1; -; mRNA.
CCDS; CCDS8000.1; -.
PIR; A26396; A26396.
RefSeq; NP_001333385.1; NM_001346456.1.
RefSeq; NP_055022.2; NM_014207.3.
UniGene; Hs.58685; -.
PDB; 2JA4; X-ray; 2.21 A; A=270-369.
PDB; 2JOP; NMR; -; A=25-134.
PDB; 2JP0; NMR; -; A=25-134.
PDB; 2OTT; X-ray; 2.50 A; X/Y=276-368.
PDBsum; 2JA4; -.
PDBsum; 2JOP; -.
PDBsum; 2JP0; -.
PDBsum; 2OTT; -.
ProteinModelPortal; P06127; -.
SMR; P06127; -.
BioGrid; 107359; 14.
DIP; DIP-21N; -.
IntAct; P06127; 4.
MINT; P06127; -.
STRING; 9606.ENSP00000342681; -.
ChEMBL; CHEMBL3712888; -.
GlyConnect; 589; -.
iPTMnet; P06127; -.
PhosphoSitePlus; P06127; -.
SwissPalm; P06127; -.
UniCarbKB; P06127; -.
BioMuta; CD5; -.
DMDM; 313104090; -.
MaxQB; P06127; -.
PaxDb; P06127; -.
PeptideAtlas; P06127; -.
PRIDE; P06127; -.
ProteomicsDB; 51869; -.
DNASU; 921; -.
Ensembl; ENST00000347785; ENSP00000342681; ENSG00000110448.
GeneID; 921; -.
KEGG; hsa:921; -.
UCSC; uc009ynk.4; human.
CTD; 921; -.
DisGeNET; 921; -.
EuPathDB; HostDB:ENSG00000110448.10; -.
GeneCards; CD5; -.
H-InvDB; HIX0009680; -.
HGNC; HGNC:1685; CD5.
HPA; CAB015392; -.
HPA; CAB020308; -.
HPA; HPA043416; -.
HPA; HPA060839; -.
MIM; 153340; gene.
neXtProt; NX_P06127; -.
OpenTargets; ENSG00000110448; -.
PharmGKB; PA26224; -.
eggNOG; ENOG410IJ3D; Eukaryota.
eggNOG; ENOG4111C54; LUCA.
GeneTree; ENSGT00390000017536; -.
HOGENOM; HOG000111490; -.
HOVERGEN; HBG005286; -.
InParanoid; P06127; -.
KO; K06455; -.
OMA; MSFHRNH; -.
OrthoDB; EOG091G0G5S; -.
PhylomeDB; P06127; -.
TreeFam; TF329295; -.
SIGNOR; P06127; -.
EvolutionaryTrace; P06127; -.
GeneWiki; CD5_(protein); -.
GenomeRNAi; 921; -.
PRO; PR:P06127; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000110448; Expressed in 101 organ(s), highest expression level in leukocyte.
CleanEx; HS_CD5; -.
ExpressionAtlas; P06127; baseline and differential.
Genevisible; P06127; HS.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
GO; GO:0038023; F:signaling receptor activity; NAS:UniProtKB.
GO; GO:0004888; F:transmembrane signaling receptor activity; NAS:UniProtKB.
GO; GO:0097190; P:apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0008283; P:cell proliferation; NAS:UniProtKB.
GO; GO:0008037; P:cell recognition; NAS:UniProtKB.
GO; GO:0031295; P:T cell costimulation; IEA:Ensembl.
Gene3D; 3.10.250.10; -; 2.
InterPro; IPR001190; SRCR.
InterPro; IPR017448; SRCR-like_dom.
InterPro; IPR036772; SRCR-like_dom_sf.
InterPro; IPR003566; Tcell_CD5.
Pfam; PF00530; SRCR; 1.
PRINTS; PR00258; SPERACTRCPTR.
PRINTS; PR01409; TCELLCD5.
SMART; SM00202; SR; 2.
SUPFAM; SSF56487; SSF56487; 2.
PROSITE; PS50287; SRCR_2; 3.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Disulfide bond;
Glycoprotein; Membrane; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 24
CHAIN 25 495 T-cell surface glycoprotein CD5.
/FTId=PRO_0000033222.
TOPO_DOM 25 372 Extracellular. {ECO:0000255}.
TRANSMEM 373 402 Helical. {ECO:0000255}.
TOPO_DOM 403 495 Cytoplasmic. {ECO:0000255}.
DOMAIN 35 133 SRCR 1. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 159 268 SRCR 2. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 276 368 SRCR 3. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
MOD_RES 439 439 Phosphoserine.
{ECO:0000244|PubMed:12522270,
ECO:0000244|PubMed:15144186}.
MOD_RES 453 453 Phosphotyrosine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 460 460 Phosphoserine.
{ECO:0000244|PubMed:12522270}.
MOD_RES 483 483 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 485 485 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
CARBOHYD 116 116 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 241 241 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 44 86 {ECO:0000255|PROSITE-ProRule:PRU00196,
ECO:0000269|PubMed:18339402}.
DISULFID 60 125 {ECO:0000255|PROSITE-ProRule:PRU00196,
ECO:0000269|PubMed:18339402}.
DISULFID 81 132 {ECO:0000255|PROSITE-ProRule:PRU00196,
ECO:0000269|PubMed:18339402}.
DISULFID 107 117 {ECO:0000255|PROSITE-ProRule:PRU00196,
ECO:0000269|PubMed:18339402}.
DISULFID 201 267 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 244 250 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 285 321 {ECO:0000255|PROSITE-ProRule:PRU00196,
ECO:0000269|PubMed:18339402}.
DISULFID 301 360 {ECO:0000255|PROSITE-ProRule:PRU00196,
ECO:0000269|PubMed:18339402}.
DISULFID 316 367 {ECO:0000255|PROSITE-ProRule:PRU00196,
ECO:0000269|PubMed:18339402}.
DISULFID 342 350 {ECO:0000255|PROSITE-ProRule:PRU00196,
ECO:0000269|PubMed:18339402}.
VARIANT 224 224 P -> L (in dbSNP:rs2241002).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_020411.
VARIANT 461 461 H -> R (in dbSNP:rs637186).
{ECO:0000244|PubMed:12522270,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:3093892,
ECO:0000269|PubMed:8740779,
ECO:0000269|Ref.3}.
/FTId=VAR_024649.
VARIANT 471 471 A -> V (in dbSNP:rs2229177).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:3093892,
ECO:0000269|PubMed:8740779,
ECO:0000269|Ref.3}.
/FTId=VAR_058203.
CONFLICT 289 289 V -> E (in Ref. 4; BAF85387).
{ECO:0000305}.
STRAND 35 37 {ECO:0000244|PDB:2JOP}.
STRAND 39 42 {ECO:0000244|PDB:2JOP}.
STRAND 45 52 {ECO:0000244|PDB:2JOP}.
STRAND 55 58 {ECO:0000244|PDB:2JOP}.
HELIX 75 77 {ECO:0000244|PDB:2JP0}.
HELIX 78 83 {ECO:0000244|PDB:2JOP}.
STRAND 86 88 {ECO:0000244|PDB:2JOP}.
STRAND 90 94 {ECO:0000244|PDB:2JOP}.
TURN 101 103 {ECO:0000244|PDB:2JOP}.
STRAND 104 110 {ECO:0000244|PDB:2JOP}.
STRAND 117 119 {ECO:0000244|PDB:2JOP}.
STRAND 122 124 {ECO:0000244|PDB:2JOP}.
STRAND 126 132 {ECO:0000244|PDB:2JOP}.
STRAND 275 280 {ECO:0000244|PDB:2JA4}.
STRAND 286 295 {ECO:0000244|PDB:2JA4}.
STRAND 298 301 {ECO:0000244|PDB:2JA4}.
HELIX 310 318 {ECO:0000244|PDB:2JA4}.
STRAND 323 331 {ECO:0000244|PDB:2JA4}.
STRAND 339 341 {ECO:0000244|PDB:2JA4}.
STRAND 344 346 {ECO:0000244|PDB:2JA4}.
HELIX 347 349 {ECO:0000244|PDB:2JA4}.
STRAND 354 356 {ECO:0000244|PDB:2JA4}.
STRAND 362 367 {ECO:0000244|PDB:2JA4}.
SEQUENCE 495 AA; 54578 MW; 9131AEC9683EE1D3 CRC64;
MPMGSLQPLA TLYLLGMLVA SCLGRLSWYD PDFQARLTRS NSKCQGQLEV YLKDGWHMVC
SQSWGRSSKQ WEDPSQASKV CQRLNCGVPL SLGPFLVTYT PQSSIICYGQ LGSFSNCSHS
RNDMCHSLGL TCLEPQKTTP PTTRPPPTTT PEPTAPPRLQ LVAQSGGQHC AGVVEFYSGS
LGGTISYEAQ DKTQDLENFL CNNLQCGSFL KHLPETEAGR AQDPGEPREH QPLPIQWKIQ
NSSCTSLEHC FRKIKPQKSG RVLALLCSGF QPKVQSRLVG GSSICEGTVE VRQGAQWAAL
CDSSSARSSL RWEEVCREQQ CGSVNSYRVL DAGDPTSRGL FCPHQKLSQC HELWERNSYC
KKVFVTCQDP NPAGLAAGTV ASIILALVLL VVLLVVCGPL AYKKLVKKFR QKKQRQWIGP
TGMNQNMSFH RNHTATVRSH AENPTASHVD NEYSQPPRNS HLSAYPALEG ALHRSSMQPD
NSSDSDYDLH GAQRL


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Tel 01 43 25 01 50

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GENTAUR GmbH
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Tel (408) 780-0908,
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Genprice Inc, Invoices and accounting
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GENTAUR Poland Sp. z o.o.


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