ID A0A226N882_CALSU Unreviewed; 2294 AA.
AC A0A226N882;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Protein-tyrosine-phosphatase {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASZ78_006971 {ECO:0000313|EMBL:OXB63479.1};
OS Callipepla squamata (Scaled quail).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Odontophoridae;
OC Callipepla.
OX NCBI_TaxID=9009 {ECO:0000313|EMBL:OXB63479.1, ECO:0000313|Proteomes:UP000198323};
RN [1] {ECO:0000313|EMBL:OXB63479.1, ECO:0000313|Proteomes:UP000198323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texas {ECO:0000313|EMBL:OXB63479.1,
RC ECO:0000313|Proteomes:UP000198323};
RC TISSUE=Leg muscle {ECO:0000313|EMBL:OXB63479.1};
RA Oldeschulte D.L., Halley Y.A., Bhattarai E.K., Brashear W.A., Hill J.,
RA Metz R.P., Johnson C.D., Rollins D., Peterson M.J., Bickhart D.M.,
RA Decker J.E., Seabury C.M.;
RT "Disparate Historic Effective Population Sizes Predicted by Modern Levels
RT of Genome Diversity for the Scaled Quail (Callipepla squamata) and the
RT Northern Bobwhite (Colinus virginianus): Inferences from First and Second
RT Generation Draft Genome Assemblies for Sympatric New World Quail.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OXB63479.1}.
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DR EMBL; MCFN01000159; OXB63479.1; -; Genomic_DNA.
DR STRING; 9009.A0A226N882; -.
DR Proteomes; UP000198323; 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; cd00063; FN3; 1.
DR CDD; cd17669; R-PTP-Z-2; 1.
DR Gene3D; 3.10.200.10; Alpha carbonic anhydrase; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
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; 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; 2.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00102; Y_phosphatase; 3.
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; 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};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000198323};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692}.
FT DOMAIN 21..253
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000259|PROSITE:PS51144"
FT DOMAIN 267..364
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1675..1971
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1913..1962
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 2002..2261
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 2178..2252
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 577..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1432..1468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1487..1559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2269..2294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1432..1454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1487..1527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1545..1559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2269..2283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2294 AA; 253514 MW; C93615E7184B1831 CRC64;
MDLADLVYGY YRQQRKLTEE VDWSYTGTLN QKNWGKKYSA CNGAKQSPIN IDADLTQVNV
NLKKLKFHGW EKETGEDTFI HNNGKTVEIN LTNDYYVSGG GLDTVFKASK ITFHWGKCNA
SSDGSEHSFE GQKFPLEIGV EDNPDYIPII NGVDSVSRFG KQAALEPFVL LNLLPNATDK
YYTYNGSLST PPCSETVEWI VFKDTVSISE RQLTVFCEVL TMQQSGYVML MDYLLNNFRE
QQYKFFGQVF SSYTGQEEIH EAVCSSEPEN VQSDPKNYTS LLVTWERPRV VYDTMIEKFA
VFYQQLDGED QTKHEFLTDG YQDLGAILNN LLPNTSYVLQ IVAVCSNGLY GKYSDQVIVD
MPLEDQEADL IPELNETEDY EDEADEKETE VDEEIAVIPS TDSAIKQIKR KDFQVTTSSY
SQENMGTKPY ESRINRYLTK EELPGEDDVF KAVYYPTSPP VSEISEEEDH FLESQKITEI
PHQRIDSTKG EEEEYIYLSS GTEPTRITTA GHSGEDFLLS PFKPDQESDD FWSSVLTTSS
AHLVTEETSQ EDILPSGSPD ISMHDVLYQG SVKYVSEGAA PSSSDEPPKH TSSTDGNVWF
HNATELTTQS LGTLDSSQLS QTSYTEAYVE GLKPATVPYS SSPVVSQDTS DVDLELPHYS
TFAFSSAELS PHSLSSSSGE YGSASAASEV LSQTTQPVYN GEIPLQPSYS SEVFPLVTPL
LFDSQMLDTT PATSDSDVTL HATPVFPSVD VSFEPTLSSY DDVPLLTFSS ASSSSKMFHR
LYTVSQMFPQ SATPAVASDK VSLHASLTLA EGDTLIQPSL AQYADVVSHQ TTRAASETLI
FGLNRTHIFS EVEPSSSDLN VHVLSTMSEH TYALSSNVGS LQSFTVSYDS AEFVHGSVDV
FHQDPLISSY NNVLVHKPSS VISQADTLLQ PTRSLSSDMD WSEAYSGSES LLPDTDTLTV
RNASSSDSVD EIAYESSGFS DVNKMLQKVD VVYGDEKELQ ISSSLSEMAS SAESKVIPEL
STSVSNNDVI KQTTSLQESL LPVSSTKGIL PVSLAFPTTK VFDYDISKLT ENHLSVQPLH
VTSPASDDTL LSPMLSAISE QAVSAPAYSK TLSSTQPYFY EASATLNNEA LLQSSFQSSG
DGTLLNTTTV VPSDPILAES SRVHKDSSAF DQILHQMAPG SATNETMLPS ASLPSVADML
SNTFSKPTAS LQGLSVSYAS EEHVSSSLFN SEDVQQVMTS LYSSDVSFQL TSLENTNAFP
PQAADAVTTP FLTADALPHV ATPPDSRTSA NVFERSEAAS VSSSSPFGFG PVQMPAVVSD
SDVSIHHTLP LPSAHISVTA VPPKSESPVT LSRLLVPSRE SSGLSPSVVS STDLWPSVVE
DDYDEYDDGF PISNCISCSS HREDQDMVVE EQNAEVNNNK DQSNLIISSH FEKPEEEERI
STAASDRQIN HAKDRHNYTS VPSLTAHEPE KHSNLTLLEN HIQTASVPLQ NTSESKSWAV
FTSDEESGSG QGTSDSLNDN ETSTDFSFPD LNERDTEGAV EAGNSELTPG SSQSSVSSVT
SDHSSVFNIS EAEASNSSHE SRIGLAESLE SEKKTVIPLV VVSALTFICL VILVGILIYW
RKCFQTAHFY LEDNTSPRVI STPPAPVFPV SDDVGAIPIK HFPKHVADLH ASNGFSEEFE
EIQSCTVDLG ITSDSSNHPD NKNKNRYINI VAYDHTRVKL AQLAEKDGKL TDYINANYVD
GYNKPKAYIA AQGPLKSTAE DFWRMIWEHN VEVIVMITNL LEKGRRKCDQ YWPAEGSEEY
GNFLVTQKSV HVLAYYTVRN FTLRNTKIKK GSQKGRSSGR VVTQYHYTQW PDMGVPEYTL
PVLTFVRKAS HAKRHAVGPI VVHCSTSPLM EHLEREPPHE FCPSGADSEE ANSAGVGRTG
TYIVLDSMLQ QIQHEGTVNI FGFLKHIRTQ RNYLVQTEEQ YIFIHDALVE AILSKETEVL
ETHIHAYVNA LLIPGPTGKT RLEKQFKLLS QSNTQQCDYS TALKQCNREK NRTSSIIPVE
RSRVGISSLS GEGTDYINAS YIMGYYQSNE FIITQHPLLH TIKDFWRMIW DHNAQLIVML
PDSQNMAEDE FVYWPNKDEP INCETFKVTM IAEEHKCLSN EEKLIIQDFI LEATQDDYVL
EVRHFQCPKW PNPDSPISKT FELISIIKEE TSNRDGPMIV HDEHGGVTAG TFCALTTLMH
QLENENSVDV YQVAKMINLM RPGVFTDIEQ YQFLYKAILS LVSTRQEENP SASMDSNGSA
LPDGNAAESL ESLV
//
