PTPRC_CYPCA
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 03-AUG-2022, entry version 100.
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 Proteomes; UP000694384; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IEA:InterPro.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.90.190.10; -; 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 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; SSF49265; SSF49265; 1.
DR SUPFAM; SSF52799; SSF52799; 2.
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
