ID F1SH38_PIG Unreviewed; 1997 AA.
AC F1SH38;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 4.
DT 27-MAR-2024, entry version 92.
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:ENSSSCP00000000535.5,
GN ECO:0000313|VGNC:VGNC:91984};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000000535.5, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000000535.5, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000000535.5,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000000535.5}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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_001926902.5; XM_001926867.6.
DR Ensembl; ENSSSCT00000000543.5; ENSSSCP00000000535.5; ENSSSCG00000000504.5.
DR GeneID; 100156181; -.
DR KEGG; ssc:100156181; -.
DR CTD; 5787; -.
DR VGNC; VGNC:91984; PTPRB.
DR eggNOG; KOG0791; Eukaryota.
DR GeneTree; ENSGT00940000156088; -.
DR HOGENOM; CLU_000787_0_0_1; -.
DR OMA; TRHQTNT; -.
DR TreeFam; TF351926; -.
DR Proteomes; UP000008227; Chromosome 5.
DR Bgee; ENSSSCG00000000504; Expressed in lung and 41 other cell types or tissues.
DR ExpressionAtlas; F1SH38; baseline and differential.
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; 16.
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; 10.
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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
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_5036468527"
FT TRANSMEM 1616..1642
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 113..205
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 291..379
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 469..561
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 642..733
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 734..820
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 821..908
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 909..1001
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1087..1175
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; 224295 MW; BD29F92A8E091B13 CRC64;
MRSHGARLAL WTALSLLQTG LGEQVRCNFT LTESRVSNRS VSLQWRTLAS PCNFSLTYSS
DTSRVAWCHP VRIDNTTYGC NPKDLQAGTI YNFRIVSLTG EEKTVVLQTD PLPPARFEVS
KEKTTSTSLH VWWTPSSGKV TWYEVQLLDD NQKTQGAQIQ ERTARNEYTF LNLTAGNKYN
IAITAISGDK RSFTIYTNGS TVPSPVKDVG ISAETNSLLI SWSRGPGNLE RYHLMLMDKG
ILVHSNTVDK STTSYAFHGL TPGHLYNVTI VTEAAGLQNY RWKPARTTPM EVSNLKVTND
GTMTSLKAKW QRPSGNVDFY NLTLSHQGTV KESRILAPHI TETQFKNLTP GRLYQVTISC
VSGELSAHKT AVGRTVPEKV GNLEANSNGS MRSLVVSWSP PAGDWEQYRI LLLNDSLVLL
NITVGKEETH YVIDEVELIP GRQYEVEVTV ESGNLKNSKR CHGRTVPMAV LQLRVKHANE
TSLSIMWQAP AAEWEKYIIS LDDRDLLIIH KSLPRDAKEF TFTDLVPGRK YKAAVTSISG
DLKNSSSTKG RTVPAQVTGL RVANQGTTSS LFTNWTHAPG DREFYQVLLI HENVVIKNES
VSSETSRYSF HSLKSGSLYS VVVTTVSGGI SSRQVVVEGR TVPSSVSGVT VNNSGRNDYL
SISWLPAPGD VDNYVVTLSH DSRVVQSLVI AKSVSECSFS SLTPGRLYNV TITTRSGKYE
NHSFGQERTV PDKVQGVSIS NSARSDYLKV SWVHATGDFD HYEVTIKNKN NFIQTKTIPK
SENECVFVKL VPGRLYSVTV STKSGQYEAS EQGNGRTIPE AVKDLTLRNR STEDLQVTWT
RADGDVDQYE IQLLFNDMKV FPSFHLVNTA TEYRFTSLTP GRQYKILVLT VSGDVQQSAF
IEGFTVPSVV KNIRVSPNGA TDSLTVNWTP GGGDVDSYTV SAFRQSQTVE SQTIPKHVSE
HTFHRLEAGE QYQILIASVS GSLKNQIEVF GRTVPASVQG IMADNAYSSH SLIVSWQKAV
GVVERYDILL LSENGILLSN ISEAATTKQH KFEDLIPGKK YKIQILTVSG GLFSKEAQTE
GRTVPAAVTN LRITENSTGH LSFSWTPSKG EFKGYNIFLY NPDGTLQERA QIDPTVQSFS
FQNLLQGRMY KMVIVTCSEE LSNESLMFGR TVPASVSNLK GSNRNMTDSL WFSWSPASGD
FDFYELILYN PNGTKKENWK DKNLTEWRFH GLIPGRKYTL CVVTHSGDLS NKVLGESRTA
PSPPSLMSFA DVANTSLAIT WKGPPDWTDY DDFELQWFPR DAITVFNPYN NRKSEGRIVY
GLRPGRSYQF SVKTVSGDSW KTYSKPVFGS VRTKPDKIQN LHCRPQNSTA ISCSWIPPDS
DFDGYSIECR KMDTQEVEFS RKLEKEKSLL NIMMLVPHKR YLVSIKVQSA GMTSEVVEDS
TITMIDRPPP PPPHIRVNKK DVLISKSSIN FTFNCSWFSD TNGAVKYFTV VVREADGSDE
LKPEQQHPLP SYLEYRHNAS IRVYQTDYFA SKCAESPDSN SKSFNIKLGA EMESLGGKCD
PNQQKFCDGP LKPRTAYRIS IRAFTQLFDE NLKEFTKPLY SDTFFSLPIT TESEPLFGVI
EGVSAGLFLI GMLVAVVALF ICRQKVNHGR ERPSARLSIR RDRPLSVHLN LGQKGNRKTS
CPIKVNQFEG HFMKLQADSN YLLSKEYEDL KDVGRNQPCD IALLPENRGK NRYNNILPYD
ASRVKLSNVD DDPCSDYINA SYIPGNNFRR EYIATQGPLP GTKDDFWKMA WEQNVHNIVM
VTQCVEKGRV KCDHYWPADQ DSLYYGDLIL QMLSESVLPE WTIREFRICS EEQLDAHRLI
RHFHYTVWPD HGVPETTQSL IQFVRTVRDY INRTPGAGPT VVHCSAGVGR TGTFIALDRI
LQQLDSKDSV DIYGAVHDLR LHRVHMVQTE CQYVYLHQCV RDVLRARKLR SEQENPLFPI
YENVNPEYHR DAGYSRH
//
