ID   PTPRC_CYPCA             Reviewed;        1216 AA.
AC   Q9IBD8;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=Receptor-type tyrosine-protein phosphatase C;
DE            EC=3.1.3.48;
DE   AltName: Full=Leukocyte common antigen;
DE   AltName: CD_antigen=CD45;
DE   Flags: Precursor;
GN   Name=ptprc;
OS   Cyprinus carpio (Common carp).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Cyprinus.
OX   NCBI_TaxID=7962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11081442; DOI=10.1006/fsim.2000.0294;
RA   Fujiki K., Shin D.H., Nakao M., Yano T.;
RT   "Molecular cloning of carp (Cyprinus carpio) leucocyte cell-derived
RT   chemotaxin 2, glia maturation factor beta, CD45 and lysozyme C by use of
RT   suppression subtractive hybridisation.";
RL   Fish Shellfish Immunol. 10:643-650(2000).
CC   -!- FUNCTION: Protein tyrosine-protein phosphatase required for T-cell
CC       activation through the antigen receptor. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10044};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08575};
CC       Single-pass type I membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Receptor class 1/6 subfamily. {ECO:0000305}.
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DR   EMBL; AB031424; BAA92179.1; -; mRNA.
DR   AlphaFoldDB; Q9IBD8; -.
DR   SMR; Q9IBD8; -.
DR   GlyCosmos; Q9IBD8; 16 sites, No reported glycans.
DR   Proteomes; UP000694384; Unplaced.
DR   Proteomes; UP000694427; Unplaced.
DR   Proteomes; UP000694700; Unplaced.
DR   Proteomes; UP000694701; Unplaced.
DR   Proteomes; UP001155660; Genome assembly.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; IEA:InterPro.
DR   CDD; cd00063; FN3; 1.
DR   CDD; cd14558; R-PTP-C-2; 1.
DR   CDD; cd14557; R-PTPc-C-1; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000242; PTP_cat.
DR   InterPro; IPR016335; Ptprc.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   PANTHER; PTHR19134; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR19134:SF539; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE C; 1.
DR   Pfam; PF00102; Y_phosphatase; 2.
DR   PIRSF; PIRSF002004; Leukocyte_common_antigen; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00194; PTPc; 2.
DR   SMART; SM00404; PTPc_motif; 2.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   PROSITE; PS50853; FN3; 3.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 2.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE   2: Evidence at transcript level;
KW   Cell membrane; Glycoprotein; Hydrolase; Membrane; Phosphoprotein;
KW   Protein phosphatase; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..1216
FT                   /note="Receptor-type tyrosine-protein phosphatase C"
FT                   /id="PRO_0000395800"
FT   TOPO_DOM        27..493
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        494..514
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        515..1216
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          71..165
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          298..395
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          401..491
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          563..819
FT                   /note="Tyrosine-protein phosphatase 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   DOMAIN          850..1129
FT                   /note="Tyrosine-protein phosphatase 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   REGION          26..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          899..919
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1154..1216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..53
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        902..917
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1154..1169
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        760
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        1070
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         728
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         760..766
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         804
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         881
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         903
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        64
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        92
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        98
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        135
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        160
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        179
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        185
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        205
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        240
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        283
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        301
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        349
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        365
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        375
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        393
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        478
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1216 AA;  138252 MW;  9D2E45F41721D2CF CRC64;
     MARFFALGPL VLVLCLVLFL SPTSTSEQDT DTKVTGSSNS PTIMQSATPT PALPTGSVKG
     VKANDSGTTE VPCQYRLIVN GYEKNSLLVN INGSKSQNYT IRIKDKKSEK KIPVSIVSDT
     TTIDILFEWL KPCTNYSVNI DNCNVVGENH FNLNVLKSVN HSAEPKGDEQ VCFKDSKWNL
     TKCVNITTED SCVQKPIQIN LETCNYTMNV HMPPVKPEIT FSESIPTKFV WSNKPLSSDN
     VTSQCKDTFK VKCTDDTEYD LDKDVFLKPS EEYTCTGKYK YYNTSIDSKS KQVNIHCEWI
     NETVFSEVTS NSIVIFWNLS PGDKCKGITW EKFSAICKKS HDQKCRKVND TTAECVFSEL
     KSYINYTCTL SAEVNKSIGV FPIYTRDFNQ RTNSSNPSFE DHDNVKVKET SHNSFNVNCK
     NLKPDEWNGP KGIYIAKLLS NRPPVTKENP KSCSFTFENL YYHTEYTIEI IAINGNKNES
     SAKATHSTRY NDKALIGFLV FLILVTSLAL LFVLYKLFLL KRKRTAEDEE ILLTQPLRRV
     EPIYAGGLVE AYKNKIADEG RLFMDEFQSI PRIFSNYTIK EAKKSENQYK NRYVDILPYD
     YNRVTLSTGG EDNYINASFI EGYREPKKYI AAQGPKDETV VDFWRMVWEQ KSSIIVMVTR
     CEEGNKTKCA QYWPSLDREA EIFEEFVVKI RSEEHCPDYV IRHLILNNKR EKGSEREVTH
     IQFISWPDHG VPGDPSLLLK LRRRVNSFKN FFSGPVVVHC SAGVGRTGTY MSIDAMIESL
     EAEGRVDIYG FVAKLRRQRC LMVQVEAQYI LIHTALIEYN QFGETEVSLS EFHSVLNTLR
     QKNGSDPSLL EKEFQKLPKF KKWRTMNTGS SEDNKKKNRD SAVIPYDFNR VIFRLDIEGN
     QTSDPEDEEE YSSDEEEESN QYINASFIDG YWCNKSLIAA QGPLQSTAEE FLLMLYQQQT
     KTLVMLTDCQ EDGKDYCFQY WGDEKKTYGD MEIEVKKTET FPTYVRRHLE IQSLKKKEVL
     KVDQYQFLKW RGRELPENAQ ELVEMASIIR ENGHYDNSKT NRNVPIVVHC NNGSSRTGIF
     CALWNLLDSA YTEKLVDVLQ EVKNLRKLRQ GMVETIEQYQ FLYTALEGAF PVQNGAVKTP
     PAKDAAQVIN ETTALLTEPN STSGADQKEA EESTAAESNE QGAKESSTAE APAAEGDGEK
     ATSEGPTNGP TATVEV
//