ID M4A7E7_XIPMA Unreviewed; 1363 AA.
AC M4A7E7;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 71.
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:ENSXMAP00000010391.2};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000010391.2, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000010391.2}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000010391.2};
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 STRING; 8083.ENSXMAP00000010391; -.
DR Ensembl; ENSXMAT00000010405.2; ENSXMAP00000010391.2; ENSXMAG00000010345.2.
DR eggNOG; KOG0789; Eukaryota.
DR GeneTree; ENSGT00940000155529; -.
DR HOGENOM; CLU_001120_2_0_1; -.
DR InParanoid; M4A7E7; -.
DR OMA; CYEAHQF; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
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 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:UP000002852};
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 702..726
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 19..283
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000259|PROSITE:PS51144"
FT DOMAIN 297..394
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 779..1047
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 964..1038
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1078..1336
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1253..1327
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 430..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1363 AA; 151916 MW; A9DE48769FF681E2 CRC64;
MSRTGGYTYR NQRKLAEDID WSYAGGLNQK HWAKKFPLCS SAKQSPININ EDLAPVKLQY
QKLRFDGWES MTTDSTTIKN DGKTVAVNVD GDFYISGGGL RSKFKVGRIT FHWGRCNASS
EGSEHSLDGV KYPLEMQIYC YEAHQFDSLD EAIQSSGRIT ALAVLFETST EDNMNYAPII
SGVNSVSRYG KSAAVSPFTL QGLLPNSTEK YFIYNGSLTT PTCDETVEWI IFKNKVAISD
DQLEMFCEVM TMQQAGYVML MDYLQNNYRD QQEQFMGQVF SSYTGIEEVQ TPVCSSEPES
IQAAPQNLSS LLVTWERPRA VYETNIEKYS ITYQLAKAED SVLSEYLTDG YQDTGAILDD
LLPNSTYEVR VVAICTNGLR GRVSDLLTVV MPFDDLENAL DPGSDETEFE GNFEPDLSWN
EVDQIRNKNL NWGTADSPRT TTSAPPWFHL SGIGTSTEES SERRTTTEPA SALISSQSEE
VLRPSEETGP ISTPLQPPED TKLPESRGNA DTGSNTLFYF TTGEPTISTS PSPLLTYTKT
DGVNVQVHHE DLSENRKVGP STVNVMAPDT KTDSSKVIFQ YPPTIESSLT TDMSSKSSPS
FKQAEIGLAQ ATSEDGTTDE NVSTHTRGFP EVQVSPSTSK TFSSTEAVHH SATSSTVPHF
SSTSVMLSGI VVQSTQPLSN DASNSSHESR VGSTSEKERK AVVPLVIIST LTLLGLVVLI
GIFIYWRMCF QTAHFYIHNM SSPRVITQSA VASTSGEDTA FLVKDFVKHV AELHSTQGFT
AEFEDVQACT VDMWMTSDSS NHPDNKTKNR YNNILAYDHS RVQLSLRASK DGKPTDYINA
NYVDGYKRPR SYIAAQGPLR SSIEDFWRMI WEQNVHIIVM ITNLVENGRR KCDQYWPAEE
QEEYGPYLVT VKSTRVLAYY THRTFRVRDT ITKKSSKKGW SNERTVEQFQ FTQWPDMGVP
ELSLPLLSFI RKSSRANTDN MGPVVVHCSA GVGRTGTYIV LDSMLKQISH EGTIDIPGFL
KHIRTQRNFL VQTEEQYIFI HDALVEAILC GDTEVLAAHL HNYVGELLTP GPSGRTRLDK
QFKLVCHSEV KQSDFSSALQ DNNSSKNRDC SVIPAERSRV CLSITAGETT DYINASFITG
YRLNREFIIT QNPLPGTIKD FWRMIWDHNI QVIISLPGTT EEAELCALRP SNEPSISFNM
FTVTQKSEAH ICLSNEDMLV VREYALSAAK DDFVLEVKHF LAPCWPNPDS PISNTFELIS
LVNEERASRD YPTVVHDDVG GVTAGTFCAL SSLKQQLEAE GSADVFQAAR LTNLLRPGVF
SDVEHYQFLY KAMLSIIGTQ EAEKTLLFSD NNGTTTDSLE SLV
//
