ID A0A3Q1FR87_9TELE Unreviewed; 1902 AA.
AC A0A3Q1FR87;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN Name=PTPRZ1 {ECO:0000313|Ensembl:ENSAPOP00000020716.1};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000020716.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000020716.1}
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 5 subfamily. {ECO:0000256|ARBA:ARBA00006246}.
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DR Ensembl; ENSAPOT00000030913.1; ENSAPOP00000020716.1; ENSAPOG00000024308.1.
DR GeneTree; ENSGT00940000155529; -.
DR Proteomes; UP000257200; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd03122; alpha_CARP_receptor_like; 1.
DR CDD; cd00063; FN3; 1.
DR CDD; cd14550; R5-PTP-2; 1.
DR Gene3D; 3.10.200.10; Alpha carbonic anhydrase; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR InterPro; IPR041887; Alpha_CARP_receptor-type.
DR InterPro; IPR001148; CA_dom.
DR InterPro; IPR036398; CA_dom_sf.
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; 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:SF461; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE ZETA; 1.
DR Pfam; PF00194; Carb_anhydrase; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00194; PTPc; 2.
DR SMART; SM00404; PTPc_motif; 2.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR SUPFAM; SSF51069; Carbonic anhydrase; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR PROSITE; PS51144; ALPHA_CA_2; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE 3: Inferred from homology;
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:UP000257200};
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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1902
FT /note="protein-tyrosine-phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018667386"
FT TRANSMEM 1232..1257
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 36..300
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000259|PROSITE:PS51144"
FT DOMAIN 314..411
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1311..1579
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1496..1570
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1610..1868
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1785..1859
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 414..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1058..1224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..433
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..841
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1066..1084
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1139..1172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1194..1224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1902 AA; 207163 MW; 7CEA4389CEF5D9B9 CRC64;
METTVCWLLL AAHFIFICQQ VGGYAYRNQR KFSEEIDWSY AGTLNQNNWA KKFPSCSNAK
QSPINIEENL AQVKLQYQKL RFDGWESLTT DRTTIKNDGK TVAVDVDGEF YVSGGALRSR
FKVGRITFHW GPCNASLDGS EHSLDGVKYP LEMQIYCYEA HRFGSLDETI KAGGRITALA
VLFETSIADN MNYASIIDGI SSVSRYGKSA EVLPFDLQGL LPNSTDKYFI YNGSLTTPPC
SETVEWIVFK NTAAISEEQL GMFCEVMTMQ QAGYVMLMDY LQNNYREQQQ QFMGQVFSSY
TGTEEVLTPV CSSEPENIQA VPYNLSSLLV TWERPRAVYD ASIEKYSVTY QLASAETSVP
SEYLTDGDQD VGAILDGLLA NTSYTVQVVA VCTNGLYGRV SDMLTFVMPV DDPENVLDPD
SDEFDDEGNY EPDLSWNEPD KIQDNDVDWS STNSQRITTS ESPFLPLPGM RTTTAQFDQR
RTTTDPVPPL RSTQSGQELT RSKEPTHHRT SSLPPEVILS KESTASADFS GADNAPVYST
TTTNKPLIAT STTPLYPITK TEGAHRSIDS KDSEKAKGGV STTTPAFIGA KAKGDKSISP
YSTTTTIMAS HTSDTSSTTL SSSSFIQVEA DPGLAIPINE DTTTHGSVST EARGLLPETR
TETSFGQPFS SSEAVLRRHT SPSMPHFSTT TTSVGLSAVL LQTTQPVSNG ESPAVFPYSS
SSSSFASSPL CDTADPSAVS STCLHDPSSS WPVLSASALD SQHVATTPLS SKGTASPAIS
TLSASTLPHL PHSSQSLSGW ETDPVFPGVG FDDSDSTGDL LSGSSGDPSV FSDTPPLQRV
PDTSDNVVAA EISESAWDPS LSTVSLPVSP TLEPSVILSP DSSATPGLSR PFSVGYEDSR
YAKGSTIESF LPEVSGDGFP LASDVDAMCG CSLEPSASSS WLHATPHVPL PSSVWDSTSL
ELYSSVGFLS TSGVAVNNRL RSLSVVGSDG LSSDQPLLSH SSISPSLTSP LSQFLQVTHS
DLPISVAATA SAVTDSWFLA SDSKTAFQTS VLPLSPTASP FSPTPEGPVL DSSSSASGSA
LFPDSQEGID QEWDRVPTSA SGESVLPYST KVSSTVPPSV TSESGQTPDD LEDHSSAFYF
ESGSGSAITS EVGGTATPTI SPVTSASPWS LGGEEESGSG HGESLFDNET SSDFSISERT
ERESEEEEAV ADASDSSHES RVGSFMDKER KAVIPLAVIS TLTVLGLIVL IGILIYWRTC
FQTAHFYIDD SSSPRVITAP PATAIASDEQ TAFPVKDFVK HVAKLHDTQA FQREFEEVQA
CTVDLGMTTD SSNHPDNKTK NRYSNILAYD HSRVRLSPQA DIDGKTTDYI NANYVDGFKK
QRSYIAAQGP LRSSTEDFWR MIWEQNVGVI VMITNLVEKG RRKCDQYWPV EGPEEYGSFM
VTVKSTRVLA YYTQRTFTVR NTHSKKGSQK GRGNERTVTQ YHYTQWPDMG VPEFALPLLS
FVRKSSKAKT NDMGPVVVHC SAGVGRTGTY IVLDSMLKQM KDEGTINITG FLKHIRTQRN
YLVQTEEQFV FIHDALVEAF LSEETEVMAA QLHRYVDELL IPGPTGRTRL DKQFKLVCHS
GVKHCDYSVA LLDCNRNKNR NSSAIPVERS RVRLSTAAGE MSDYINASYI TGYRQSSEFI
ITQNPLPGTI KDFWTMIWEH NAQVIVSLPW VEEEAELCIF WPRKGQPISY EMFTVTQRSE
THICLSNEDM LVVHDYVLEA TQDDFVLEVK HFHAPPWPNP DSPISNTFEL VNLVKRESAA
KDGPTVVHDD VGGVTAGTFC ALSSLTNQLD TERSVDVFQV AKLTNLMRPG IFSDIEQYQF
LYKAMLSLIG TQEDEKTLQS SDNNGTIVVG TASTAESLES LV
//
