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Database: UniProt
Entry: A0A3B4FD17_9CICH
LinkDB: A0A3B4FD17_9CICH
Original site: A0A3B4FD17_9CICH 
ID   A0A3B4FD17_9CICH        Unreviewed;      2012 AA.
AC   A0A3B4FD17;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
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:ENSPNYP00000007883.1};
OS   Pundamilia nyererei.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX   NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000007883.1, ECO:0000313|Proteomes:UP000261460};
RN   [1] {ECO:0000313|Ensembl:ENSPNYP00000007883.1}
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   STRING; 303518.ENSPNYP00000007883; -.
DR   Ensembl; ENSPNYT00000008076.1; ENSPNYP00000007883.1; ENSPNYG00000006016.1.
DR   GeneTree; ENSGT00940000156088; -.
DR   Proteomes; UP000261460; Unplaced.
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; 10.
DR   CDD; cd14617; R-PTPc-B; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 14.
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:SF3; PROTEIN-TYROSINE-PHOSPHATASE; 1.
DR   Pfam; PF00041; fn3; 14.
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; 13.
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   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   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..2012
FT                   /note="protein-tyrosine-phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017254355"
FT   DOMAIN          128..219
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          304..394
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          483..572
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          573..661
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          662..756
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          923..1013
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1014..1103
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1104..1194
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1281..1374
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1375..1469
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1736..1996
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1911..1987
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          372..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2012 AA;  221141 MW;  A504D028B5A907CD CRC64;
     MLRCAATCLI LGFVWGAKTV QTSEGPRCSA DLKEISSSSD SIAVQVTSAG LSCNFSLFCI
     LDSWSSPAHC KSDGETSSAT ICNITGLQPG TVYQLTAVSR KDGEISHGTV QTDPVGPAHL
     DLQLDPAQPH HKSLFMVLSS SALTVSWTQS TGRVDWYDVT LEDTSSGFRR RTRIKGSAAS
     QTGFTSLIPG TLYKVSVVAS AGNKSASPVH AMTATAPSSV DGLQVASSSS HSLGVTWWIG
     SGRTENLRVL LRDRAGVLLK NITLKNSSTS AELDGLHPGT PYTITVVTEA VGLQSSASTA
     SVTAPAQVSR LVLENNGSSD HLRASWLPPK GGVESYLVTL RAPGSDTQLR HLLPNITQVE
     FEGLTPGRSY EVSVSSSAGS QSTESRSTAR TVPDQVSALS MSADARTLWL RWLPPRGDWE
     NYSVILKNGS VVLANETVSK ASRQHAFSVL SLVPGRLYSA EVTVHSGVLS NTARCSSQLA
     PWPVQQLLVR QADETSLSVR WSRPPGQWDG FTVLLRWATA AATIVDQRVL GWEAKECTFN
     SITPGGQYII TVTTNSGNLS SSASVTARTT PAQVSGLRLS NLGSTDSLQA RWAPASGYLD
     SYQVLLVHDS SVIKNESVMA NISSLSFQAL RPGALYRVVV TTVRVGHISR QTVSEGRTVP
     AAVSDVRVSN NGRMDFLSVS WSQAVGEVDR YLVTLSDRER TIHTLTVPKS TPTCVFDSLV
     SGRLYNISIT TCSGLYKNQT FIQERTQPSK VQSPTATHNA SDSYLKVYWR HAAGDFDLYQ
     VFIKHNNVFL QNKTVPKTEH NCVFTGLVPG RLYTVLVTTW SGKYEAIAST HGSTFPAAVR
     SLTLAGRGTE DLRVTWMAAP GDVDHYEVQL LFSDMKVFPP ITLGSGVRDC VLSSLTPGRL
     YKIIVSTYSG TNQKARYIEG RTVPSKVKNI HISNSGDSSS LMVSWTPGPG DVDGFSVFLY
     RESRKLSTRS VLKHQNEVTF GSLQPGQVYT IMVQSVSGDL VNNNTVTGRT VPSAVTGLQV
     DSHHTTCSIQ VSWQEALGVA DGYVLQVLDD RGSMVRNVSQ HFGHTWQQFD GLTPGKKYRV
     VVQTTSGGVH SVGVSTEART NPAVVTNLAV TANTTTSLSF HWSPPEGDFQ LYEVFLYDRN
     DQLHEKKRVQ SNSQQCTFQG LRPGAPYKML IQIHSGDQTN QTSIYTRTVP SAAAFLKAKS
     GNQSDSLWVN WEHGGGDLSG YQLYLYNPNG SQQAMHQLGS EATGFIFSGL VAGRLYRAEV
     LSQSGGLSNR ASTLGRTAPR PPASILFRGV TNTSLEITWS GPVDSDYDDF DLQWTPRDRL
     SIINPYHTRT SSNRILRGMF PGRLYNFSLR TVSGTTEPGA TPTYSTPIRK SIRTKPERVH
     SLHCRPQSST SISCSWVTPD TDYDSYTIEC LHKDSHTLMY SRLAEQDSNS YIITELEPHK
     HYTVSVKVMS GGKPSDEAQD NVVTMLDRPP VPPSGTRVSE QSAVVTKSSI SFQFNCSWFS
     DVNGAVKYFT VVVTESEDVS LMQLEQKHPL PSYLDYSSNS SIRSYQTSYF PSRCTESPDS
     TTQSFNITLG TGMDLLGGTC DARGSDQDPE SSGELNHFCD GPLKPKTAYR ISVRAFTQLF
     DDDAKDLSVL SPLFSDTCLS QPIITEAEPL SGVIEGVSAG LFLAAVIVGI TALFVCRHRT
     RKVEEERLEV RINMRRERAA AGNQLGVRGR RISSPIKIVN FESHYSKLQA DSNYLMSEEY
     EDLKDVGRNQ PLDSALLPEN RGKNRYNNIL PYDSTRVKLS YVDDDPCSDY INASYIPGNS
     FRREYIATQG PLPGTKDDFW KMVWEQNVHN VVMVTQCVEK GRVKCDHYWP FDQDPLYYGD
     LIVQMLSESV LPEWTIREFN IYSEEQLGFS RLVRQFHYTV WPDHGVPETT QSLIQFVRTV
     RDYVNRTSGS GATVVHCSAG VGRTGTFIVL DRVLQQLDAK DTVDIYSAVF DLRLHRSHMV
     QTEVQYAYLH QCVRDVLRAR KLRSEQEGMY RM
//
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