ID A0A2K6L9I3_RHIBE Unreviewed; 2304 AA.
AC A0A2K6L9I3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 39.
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:ENSRBIP00000020210.1};
OS Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000020210.1, ECO:0000313|Proteomes:UP000233180};
RN [1] {ECO:0000313|Ensembl:ENSRBIP00000020210.1, ECO:0000313|Proteomes:UP000233180}
RP NUCLEOTIDE SEQUENCE.
RA Wu, C.-I. and Zhang, Y.;
RT "Genome of Rhinopithecus bieti.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSRBIP00000020210.1}
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 5 subfamily. {ECO:0000256|ARBA:ARBA00006246}.
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DR STRING; 61621.ENSRBIP00000020210; -.
DR Ensembl; ENSRBIT00000044088.1; ENSRBIP00000020210.1; ENSRBIG00000034085.1.
DR GeneTree; ENSGT00940000155529; -.
DR OMA; DPINCES; -.
DR Proteomes; UP000233180; Unplaced.
DR GO; GO:0072534; C:perineuronal net; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0005178; F:integrin binding; IEA:Ensembl.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR GO; GO:0007611; P:learning or memory; IEA:Ensembl.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IEA:Ensembl.
DR GO; GO:0031641; P:regulation of myelination; IEA:Ensembl.
DR GO; GO:0070445; P:regulation of oligodendrocyte progenitor proliferation; IEA:Ensembl.
DR CDD; cd03122; alpha_CARP_receptor_like; 1.
DR CDD; cd00063; FN3; 1.
DR CDD; cd17669; R-PTP-Z-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:UP000233180};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1626..1651
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 18..282
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000259|PROSITE:PS51144"
FT DOMAIN 296..395
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1706..1981
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1898..1972
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 2012..2271
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 2188..2262
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 463..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1385..1512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1532..1565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..629
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1403..1422
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1451..1502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1533..1558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2304 AA; 253981 MW; 28C73A4B56E490D5 CRC64;
VDWANGYYRQ QRKLVEEIGW SYTGALNQKN WGKKYPTCNS PKQSPINIDE DLTQVNVNLK
KLKFQGWDKT SLENTFIHNT GKTVEINLTN DYRVSGGVSE MVFKASKITF HWGKCNMSSD
GSEHSLEGQK FPLEMQIYCF DADRFSSFEE AVKGKGKLRA LSILFEVGTE ENLDFKAIID
GVESVSRFGK QAALDPFILL NLLPNSTDKY YVYNGSLTSP PCTDTVDWIV FKDTVSISEN
QLAVFCEVLT MQQSGYVMLM DYLQNNFREQ QYKFSRQVFS SYTGKEEIHE AVCSSEPENV
QADPENYTSL LVTWERPRVV YDTMIEKFAV LYQQLDGEDQ TKHEFLTDGY QDLGAILNNL
LPNMSYVLQI VAICTNGLYG KYSDQLIVDM PTDNPGKFFL LFPYDSLNLV CFSKEEEEGK
DVEEDTIVNP GRDSATNQIR KKEPQISTTT HYNRIRTKYN EAKTNRSPTR GSEFSGKGDV
PNTSLNSTSQ SVTKLATEKD ISLTSQTVTE LPPHTVEGTS ASLNNGSKTV LRSPHMNLSG
TVESLNTVSI TEYEEESLLT SFKLDTGAED SSGSSPATSA IPFISENISQ GYIFSSENPE
TITYDVLIPE SARNASEDST SSGSEESLKD PSVEGNVWFP SFTDVTAQPD VGSGRESFLQ
TNYTEIRVDE SEKTTKSFSA GPVMSQGPSV TDLEMPHYST FAYFPTEVTP HAFTPSSRQQ
DLVSTVNVVH SQTTQPVYNG ETPLQPSYSS EVFPLVTPLL LDNQILNTTP AASSSDSALH
ATPVFPSVDV SFESILSSYD GAPLLPFSSA SFSSELFRHL HTVSQILPQV TSATESDKVP
LHASLPVAGG DLLLEPSLVQ YSDVLSHLTT THAASETLEF GSESGVLYKT LMFSQVEPPS
SDAMMHARSS GPEPSYALSN NEGSQHIFTV SYSSAIPVHD SVGVTYQGSL FSGPSHIPIP
KSSLITPTAS LLQPTHALSG DGEWSGDSSD SEFLLPDTDG LTALNISSPV SVAEFTHTTS
VFGDDNKALS KSEIIYGNET EWQILSFNEM VYPSESTVMP NMHDNVNKLN ASLQETSVSI
SSTKGMFPGS LAHTTTKVFD HEISQVPENN FSVQPTHTVF QASGDTSLKP VLSANSEPAS
SDPASSEMLS PSTQLLFYET SASFSTEVLL QPSFQASDVD TLLKTVLPAV SSDPILVETP
KVDKISSTIL HLIVSNSASS ENVLHSTSVP GFDVSPTSHM HSASLQGLTI SYASEKYEPI
LFKSESSHQV VPSLYSNDEL FQTANLEIKQ AYPPKGRHEF ATPVLSIDEQ LNTLINKFIH
SDEILTSTKS SVTDKVFAGI PTVASDTFVS TDHSVPIGNG HVAITAVSPN RDGSVTTTKL
LFPSKATSEL SHSTRSDADL VGGGEDGDTD DDDGDDDDDD RDSDGLSIHK CMSCSSYRES
QEKVMNDSDT HENSLMDQNN PVSYSLSENS EEDNRVTSVS PDSQTGVDRS PGKSPSANGL
SQKHNDGKEE NDIQTGSALL PLSPESKAWA VLTSDEESGS GQGTSDSLNE NETSTDFSFP
DTNEKDADGI LAAGDSEITP GFPQSPTPSV TSENSEVFHV SEAEASNSSH ESRIGLAEGL
ESEKKAVIPL VIVSALTFIC LVVLVGILIY WRKCFQTAHF YLEDSTSPRV ISTPPTPIFP
ISDDVGAIPI KHFPKHVADL HASSGFTEEF ETLKEFYQEV QSCTVDLGIT ADSSNHPDNK
HKNRYINIVA YDHSRVKLAQ LAEKDGKLTD YINANYVDGY NRPKAYIAAQ GPLKSTAEDF
WRMIWEHNVE VIVMITNLVE KGRRKCDQYW PADGSEEYGN FLVTQKSVQV LAYYTVRNFS
LRNTKIKKGS QKGRPSGRVV TQYHYTQWPD MGVPEYSLPV LTFVRKAAYA KRHAVGPVVV
HCSAGVGRTG TYIVLDSMLQ QIQHEGTVNI FGFLKHIRSQ RNYLVQTEEQ YVFIHDTLVE
AILSKETEVL DSHIHAYVNA LLIPGPTGKT KLEKQFQLLS QSNIQQSDYS TALKQCNREK
NRTSSIIPVE RSRVGISSLS GEGTDYINAS YIMGYYQSNE FIITQHPLLH TIKDFWRMIW
DHNAQLVVMI PDGQNMAEDE FVYWPNKDEP INCESFKVTL MAEEHKCLTN EEKLIIQDFI
LEATQDDYVL EVRHFQCPKW PNPDSPISKT FELISVIKEE AANRDGPMIV HDEHGGVTAG
TFCALTTLMH QLEKENSVDV YQVAKMINLM RPGVFADIEQ YQFLYKVILS LVSTRQEENP
STSLDSNGAA LPDGNIAESL ESLV
//
