ID   CD82_RAT                Reviewed;         266 AA.
AC   O70352;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 113.
DE   RecName: Full=CD82 antigen;
DE   AltName: Full=Metastasis suppressor Kangai-1 homolog;
DE   AltName: CD_antigen=CD82;
GN   Name=Cd82; Synonyms=Kai1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RX   PubMed=9831222;
RX   DOI=10.1002/(sici)1097-0045(19981201)37:4<253::aid-pros7>3.0.co;2-3;
RA   Suzuki H., Dong J.T., Gao A.C., Barrett J.C., Isaacs J.T.;
RT   "Identification of the rat homologue of KAI1 and its expression in Dunning
RT   rat prostate cancers.";
RL   Prostate 37:253-260(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 137-148; 170-189 AND 254-262, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RA   Lubec G., Kang S.U., Lubec S.;
RL   Submitted (SEP-2007) to UniProtKB.
RN   [3]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-157, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=24090084; DOI=10.1021/pr400783j;
RA   Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA   Graham M.E., Packer N.H., Cordwell S.J.;
RT   "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT   heterogeneity.";
RL   J. Proteome Res. 12:5791-5800(2013).
CC   -!- FUNCTION: Associates with CD4 or CD8 and delivers costimulatory signals
CC       for the TCR/CD3 pathway. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts directly with IGSF8. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P27701};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family. {ECO:0000305}.
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DR   EMBL; AF049882; AAC05159.1; -; mRNA.
DR   AlphaFoldDB; O70352; -.
DR   SMR; O70352; -.
DR   STRING; 10116.ENSRNOP00000000052; -.
DR   GlyGen; O70352; 5 sites, 4 N-linked glycans (1 site).
DR   iPTMnet; O70352; -.
DR   PhosphoSitePlus; O70352; -.
DR   PaxDb; O70352; -.
DR   PRIDE; O70352; -.
DR   UCSC; RGD:69070; rat.
DR   RGD; 69070; Cd82.
DR   eggNOG; KOG3882; Eukaryota.
DR   InParanoid; O70352; -.
DR   PhylomeDB; O70352; -.
DR   PRO; PR:O70352; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   Gene3D; 1.10.1450.10; -; 1.
DR   InterPro; IPR018499; Tetraspanin/Peripherin.
DR   InterPro; IPR000301; Tetraspanin_animals.
DR   InterPro; IPR018503; Tetraspanin_CS.
DR   InterPro; IPR008952; Tetraspanin_EC2_sf.
DR   PANTHER; PTHR19282; PTHR19282; 1.
DR   Pfam; PF00335; Tetraspanin; 1.
DR   PIRSF; PIRSF002419; Tetraspanin; 1.
DR   SUPFAM; SSF48652; SSF48652; 1.
DR   PROSITE; PS00421; TM4_1; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; Glycoprotein; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..266
FT                   /note="CD82 antigen"
FT                   /id="PRO_0000219228"
FT   TOPO_DOM        1..11
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        33..53
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        54..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        73..83
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        84..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        111..227
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        228..249
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        250..266
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        127
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        131
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        157
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0007744|PubMed:24090084"
FT   CARBOHYD        166
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        197
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   266 AA;  29487 MW;  D6E10AB5AA348474 CRC64;
     MGAGCVKVTK YFLFLFNLLF FILGAVILGF GVWILADKSS FISVLQTSSS SLQVGAYVFI
     GVGAITMLMG FLGCIGAVNE VRCLLGLYFV FLLLILIAQV TVEVLFYFNA NKLKQEMGNT
     VMDIIQNYSV NASSSREEAW DYVQAQVKCC GWVSPSNWTR NPVLKNSTKT TYPCSCEKTK
     EEDNQLIVKK GFCESDNSTA SENSPEDWPV HPEGCMEKAQ AWLQENFGIL LGVCAGVAVI
     ELLGLFLSIC LCRYIHSEDY SKVPKY