CD7_HUMAN
ID CD7_HUMAN Reviewed; 240 AA.
AC P09564;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=T-cell antigen CD7;
DE AltName: Full=GP40;
DE AltName: Full=T-cell leukemia antigen;
DE AltName: Full=T-cell surface antigen Leu-9;
DE AltName: Full=TP41;
DE AltName: CD_antigen=CD7;
DE Flags: Precursor;
GN Name=CD7;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PALMITOYLATION AT CYS-198.
RX PubMed=3501369; DOI=10.1002/j.1460-2075.1987.tb02651.x;
RA Aruffo A., Seed B.;
RT "Molecular cloning of two CD7 (T-cell leukemia antigen) cDNAs by a COS cell
RT expression system.";
RL EMBO J. 6:3313-3316(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1703303; DOI=10.1073/pnas.88.2.603;
RA Schanberg L.E., Fleenor D.E., Kurtzberg J., Haynes B.F., Kaufman R.E.;
RT "Isolation and characterization of the genomic human CD7 gene: structural
RT similarity with the murine Thy-1 gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:603-607(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 205-240.
RX PubMed=1711009; DOI=10.1007/bf00216694;
RA Yoshikawa K., Seto M., Ueda R., Obata Y., Notake K., Yokochi T.,
RA Takahashi T.;
RT "Molecular cloning of the gene coding for the human T cell differentiation
RT antigen CD7.";
RL Immunogenetics 33:352-360(1991).
RN [6]
RP TOPOLOGY.
RX PubMed=2479685;
RA Ware R.E., Scearce R.M., Dietz M.A., Starmer C.F., Palker T.J.,
RA Haynes B.F.;
RT "Characterization of the surface topography and putative tertiary structure
RT of the human CD7 molecule.";
RL J. Immunol. 143:3632-3640(1989).
RN [7]
RP INTERACTION WITH SECTM1.
RX PubMed=10652336; DOI=10.1074/jbc.275.5.3431;
RA Lyman S.D., Escobar S., Rousseau A.-M., Armstrong A., Fanslow W.C.;
RT "Identification of CD7 as a cognate of the human K12 (SECTM1) protein.";
RL J. Biol. Chem. 275:3431-3437(2000).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-96.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-96.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
CC -!- FUNCTION: Not yet known.
CC -!- SUBUNIT: Interacts with SECTM1. {ECO:0000269|PubMed:10652336}.
CC -!- INTERACTION:
CC P09564; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-2836587, EBI-8652744;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
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DR EMBL; X06180; CAA29546.1; -; mRNA.
DR EMBL; M37271; AAA51953.1; -; Genomic_DNA.
DR EMBL; BT006696; AAP35342.1; -; mRNA.
DR EMBL; BC009293; AAH09293.1; -; mRNA.
DR EMBL; BC013297; AAH13297.1; -; mRNA.
DR EMBL; D00749; BAA00646.1; -; Genomic_DNA.
DR CCDS; CCDS11807.1; -.
DR PIR; A39016; A39016.
DR RefSeq; NP_006128.1; NM_006137.6.
DR AlphaFoldDB; P09564; -.
DR SMR; P09564; -.
DR BioGRID; 107362; 23.
DR IntAct; P09564; 8.
DR MINT; P09564; -.
DR STRING; 9606.ENSP00000312027; -.
DR GlyGen; P09564; 2 sites.
DR iPTMnet; P09564; -.
DR PhosphoSitePlus; P09564; -.
DR SwissPalm; P09564; -.
DR BioMuta; CD7; -.
DR DMDM; 116031; -.
DR jPOST; P09564; -.
DR MassIVE; P09564; -.
DR PaxDb; P09564; -.
DR PeptideAtlas; P09564; -.
DR PRIDE; P09564; -.
DR ProteomicsDB; 52247; -.
DR ABCD; P09564; 9 sequenced antibodies.
DR Antibodypedia; 3610; 1992 antibodies from 53 providers.
DR DNASU; 924; -.
DR Ensembl; ENST00000312648.8; ENSP00000312027.3; ENSG00000173762.8.
DR GeneID; 924; -.
DR KEGG; hsa:924; -.
DR MANE-Select; ENST00000312648.8; ENSP00000312027.3; NM_006137.7; NP_006128.1.
DR CTD; 924; -.
DR DisGeNET; 924; -.
DR GeneCards; CD7; -.
DR HGNC; HGNC:1695; CD7.
DR HPA; ENSG00000173762; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 186820; gene.
DR neXtProt; NX_P09564; -.
DR OpenTargets; ENSG00000173762; -.
DR PharmGKB; PA26234; -.
DR VEuPathDB; HostDB:ENSG00000173762; -.
DR eggNOG; ENOG502SD5I; Eukaryota.
DR GeneTree; ENSGT00390000013965; -.
DR HOGENOM; CLU_115462_0_0_1; -.
DR InParanoid; P09564; -.
DR OMA; VYEDMSC; -.
DR OrthoDB; 1083212at2759; -.
DR PhylomeDB; P09564; -.
DR TreeFam; TF338565; -.
DR PathwayCommons; P09564; -.
DR SignaLink; P09564; -.
DR BioGRID-ORCS; 924; 14 hits in 1066 CRISPR screens.
DR GeneWiki; CD7; -.
DR GenomeRNAi; 924; -.
DR Pharos; P09564; Tbio.
DR PRO; PR:P09564; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P09564; protein.
DR Bgee; ENSG00000173762; Expressed in granulocyte and 110 other tissues.
DR ExpressionAtlas; P09564; baseline and differential.
DR Genevisible; P09564; HS.
DR GO; GO:0016021; C:integral component of membrane; TAS:UniProtKB.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
DR GO; GO:0038023; F:signaling receptor activity; TAS:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0006955; P:immune response; TAS:UniProtKB.
DR GO; GO:0042110; P:T cell activation; TAS:UniProtKB.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; NAS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR039090; CD7.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR PANTHER; PTHR15343; PTHR15343; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Adaptive immunity; Disulfide bond; Glycoprotein; Immunity;
KW Immunoglobulin domain; Lipoprotein; Membrane; Palmitate; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT CHAIN 26..240
FT /note="T-cell antigen CD7"
FT /id="PRO_0000014633"
FT TOPO_DOM 26..180
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:2479685"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 202..240
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:2479685"
FT DOMAIN 26..130
FT /note="Ig-like"
FT REPEAT 145..153
FT /note="1"
FT REPEAT 154..162
FT /note="2"
FT REPEAT 163..171
FT /note="3"
FT REPEAT 172..180
FT /note="4"
FT REGION 140..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..180
FT /note="4 X 9 AA tandem repeats, potential spacer function"
FT LIPID 198
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:3501369"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:19349973"
FT DISULFID 35..142
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 48..114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VARIANT 113
FT /note="T -> A (in dbSNP:rs34579511)"
FT /id="VAR_049855"
SQ SEQUENCE 240 AA; 25409 MW; EBBCE08279552108 CRC64;
MAGPPRLLLL PLLLALARGL PGALAAQEVQ QSPHCTTVPV GASVNITCST SGGLRGIYLR
QLGPQPQDII YYEDGVVPTT DRRFRGRIDF SGSQDNLTIT MHRLQLSDTG TYTCQAITEV
NVYGSGTLVL VTEEQSQGWH RCSDAPPRAS ALPAPPTGSA LPDPQTASAL PDPPAASALP
AALAVISFLL GLGLGVACVL ARTQIKKLCS WRDKNSAACV VYEDMSHSRC NTLSSPNQYQ
