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   27-MAR-2024, entry version 203.
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   GlyCosmos; P09564; 2 sites, No reported glycans.
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; 9606-ENSP00000312027; -.
DR   PeptideAtlas; P09564; -.
DR   ProteomicsDB; 52247; -.
DR   ABCD; P09564; 9 sequenced antibodies.
DR   Antibodypedia; 3610; 2219 antibodies from 54 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   AGR; HGNC:1695; -.
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; SACVVYE; -.
DR   OrthoDB; 5321775at2759; -.
DR   PhylomeDB; P09564; -.
DR   TreeFam; TF338565; -.
DR   PathwayCommons; P09564; -.
DR   SignaLink; P09564; -.
DR   BioGRID-ORCS; 924; 15 hits in 1144 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 111 other cell types or tissues.
DR   ExpressionAtlas; P09564; baseline and differential.
DR   GO; GO:0016020; C:membrane; TAS:UniProtKB.
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   CDD; cd00099; IgV; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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; CD7; 1.
DR   PANTHER; PTHR15343:SF0; T-CELL ANTIGEN CD7; 1.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00406; IGv; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   Genevisible; P09564; HS.
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
//