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Database: UniProt
Entry: A0A2K5M668_CERAT
LinkDB: A0A2K5M668_CERAT
Original site: A0A2K5M668_CERAT 
ID   A0A2K5M668_CERAT        Unreviewed;      1997 AA.
AC   A0A2K5M668;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   Name=PTPRB {ECO:0000313|Ensembl:ENSCATP00000020676.1};
OS   Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Cercocebus.
OX   NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000020676.1, ECO:0000313|Proteomes:UP000233060};
RN   [1] {ECO:0000313|Ensembl:ENSCATP00000020676.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00001490};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Receptor class 3 subfamily. {ECO:0000256|ARBA:ARBA00025789}.
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DR   RefSeq; XP_011905090.1; XM_012049700.1.
DR   Ensembl; ENSCATT00000044868.1; ENSCATP00000020676.1; ENSCATG00000033946.1.
DR   GeneID; 105581022; -.
DR   CTD; 5787; -.
DR   GeneTree; ENSGT00940000156088; -.
DR   OMA; TRHQTNT; -.
DR   OrthoDB; 5402037at2759; -.
DR   Proteomes; UP000233060; Unplaced.
DR   Bgee; ENSCATG00000033946; Expressed in lung and 12 other cell types or tissues.
DR   GO; GO:0016020; C: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   CDD; cd00063; FN3; 14.
DR   CDD; cd14617; R-PTPc-B; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 15.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
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; IPR041201; PTPRJ_TM.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   PANTHER; PTHR46957; CYTOKINE RECEPTOR; 1.
DR   PANTHER; PTHR46957:SF2; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE BETA; 1.
DR   Pfam; PF00041; fn3; 16.
DR   Pfam; PF18861; PTP_tm; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 17.
DR   SMART; SM00194; PTPc; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 16.
DR   PROSITE; PS50853; FN3; 9.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE   3: Inferred from homology;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..1997
FT                   /note="protein-tyrosine-phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014393983"
FT   DOMAIN          113..208
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          292..379
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          470..556
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          643..734
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          735..821
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          822..912
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          995..1087
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1260..1356
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1357..1448
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1703..1963
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1878..1954
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
SQ   SEQUENCE   1997 AA;  224201 MW;  EFD3A3F890791E07 CRC64;
     MLSHGAELAL WIALSLLQTG LAEPERCNFT LAESKASSHS VSIRWRIWGS PCNFNLTYSS
     DTLGAASCPP FRLDNTTYGC NLQDLQAGTI YNFRIVSLDG EERTVVLQTD PLPPARFGVS
     KEKSTSTSLH IWWTPSPGKV TSYEVQLFDE NNRKIQGVQI QESTSWNKYT FFNLTAGSKY
     NITITAVSGG KHSSSVYTNG STVPSPVEDI GISTKANSLL VSWSHGSGNV ERYRLMLMDK
     GILVHGSVVD RQATSYAFNG LTPGYLYNLT VVTEAAGLQN YKWKLVRTAP MEVSNLKVTN
     DGSLTSLKVK WQRPPGNVDS YNITLSHKGT IKESRVLAPR VTETHFKELT PGRLYQVTVS
     CGSGELSAQR MAVGRTFPDK VANLEANSNG WMRSLVVSWS PPAGDWEQYR ILLFNDSVVL
     LNITVGKEET QYVMDDMGLV PGRQYEVEVI VESGNLKNPE RCQGRTVPLA VLQLRVKHAN
     ETSLSIIWQP PVAEWEEYII SLADRDLRLI HKSLSKDAKE FTFTDLVPGR KYMATVTSIS
     GDLKNSSSVK GRTVPAQVTD LHVANQGMTS SLFTNWTQAQ GDVEFYQVLL IHENVVIKNE
     SISSEASGYS FHPLKSGSLY SVVVTTVSGG ISSRQVVVEG RTVPSSVSGV TVNNSGRNDY
     LSVSWLPAPG DVDNYEVTLS HDGRVVQSLV IAKSVRECSF SSLTPGRLYT VTVTTRSGKY
     ENHSFSQERT VPDKVQGVSV SNSARSDYLR VSWVHATGDF DHYEVTIKNK NNFIETKSIP
     KSENECVFVQ LVPGRLYSVT VTTKSGQYEA SEQGNGRTIP EPVKDLTLRN RSTEDLHVTW
     SGANGDVDQY EIQLLFNDMK VFPPFHLVNT ATEYRFTSLT PGRQYKILVL TISGDVQQSA
     FIEGFTVPSA VKNIHISPNG ATDSLTVNWT PGGGDVDSYT VSAFRHSQKV DSQTVPKHIF
     EHTFHRLEAG EQYQIMIASV SGSLKNQINV VGRTVPASVQ GVIADNAYSS HSLIVSWQKA
     AGVAERYDIL LLTENGILHN TSEPATTKQH KFEDLIPGKK YKIQILTVSG GLFSKEAQTE
     GRTVPAAVTN LRITENSTRH LSFRWTASEG ELSWYNIFLY NPDGNLQERA QVDPQVQSFS
     FQNLLQGRMY KMVIVTHSGE LSNESFIFGR TVPASVSHLR GSNRNMTDSL WFSWSPASGD
     FDFYELILYN PNGTKKENWK DKDLTEWRFH GLVPGRKYTL WVVTHSGDLS NKVTVESRTA
     PSPPSLMSFA DIANTSLAIT WKGPPDWTDY NDFELQWLPR DALTVFNPYN NRKSEGRILY
     GLRPGRSYQF SVKTVSGDSW KTYSKPIFGT VRTKPDKIQN LHCRPQNSTA IACSWIPPDS
     DFDGYSIECR KMDTQEVEFS RKLEKEKSLL NIMMLVPHKR YLVSIKVQSA GMTSEVVEDS
     TITMIDRPPP PPPHIRVNEK DVLISKSSIN FTVNCSWFSD TNGAVKYFTV VVREADGSDE
     LKPEQQHPLP SYLEYRHNAS IRVYQTNYFA SKCAENPNSN SKSFNIKLGA EMESLGGKCD
     PTQQKFCDGP LKPHTAYRIS IRAFTQLFDE DLKEFTKPLY SDTFFSLPIT TESEPLFGAI
     EGVSAGLFLI GMLVAVVALL ICRQKVSHGR ERPSARLSIR RDRPLSVHLN LGQKGNRKTS
     CPIKINQFEG HFMKLQADSN YLLSKEYEEL KDVGRNQSCD IALLPENRGK NRYNNILPYD
     ATRVKLSNVD DDPCSDYINA SYIPGNNFRR EYIVTQGPLP GTKDDFWKMV WEQNVHNIVM
     VTQCVEKGRV KCDHYWPADL DSLYYGDLIL QMLSESVLPE WTIREFKICS EEQLDAHRLI
     RHFHYTVWPD HGVPETTQSL IQFVRTVRDY INRSPGAGPT VVHCSAGVGR TGTFIALDRI
     LQQLDSKDSV DIYGAVHDLR LHRVHMVQTE CQYVYLHQCV RDVLRARKLR SEQENPLFPI
     YENVNPEYHR DPVYSRH
//
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