ID A0A498MFZ9_LABRO Unreviewed; 2004 AA.
AC A0A498MFZ9;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN ORFNames=ROHU_007469 {ECO:0000313|EMBL:RXN19070.1};
OS Labeo rohita (Indian major carp) (Cyprinus rohita).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Labeoninae; Labeonini; Labeo.
OX NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN19070.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN19070.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN19070.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN19070.1};
RA Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA Shah T.M., Rai A., Jena J.K.;
RT "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL Submitted (MAR-2018) 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:RXN19070.1}.
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DR EMBL; QBIY01012686; RXN19070.1; -; Genomic_DNA.
DR STRING; 84645.A0A498MFZ9; -.
DR Proteomes; UP000290572; 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 1: Evidence at protein level;
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 Proteomics identification {ECO:0007829|PeptideAtlas:A0A498MFZ9};
KW Receptor {ECO:0000313|EMBL:RXN19070.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000290572};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..2004
FT /note="protein-tyrosine-phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019770631"
FT DOMAIN 40..304
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000259|PROSITE:PS51144"
FT DOMAIN 318..415
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1394..1678
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1592..1669
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1709..1970
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1887..1961
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 539..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 912..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1232..1328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1979..2004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1272..1298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2004 AA; 220196 MW; 7A5085A79715E890 CRC64;
MEAFATRCAL FLAQIALFSN TVDVSEAYGF RSQKKLSENI DWSYAGTLNQ NNWAKKYPSC
NNAKQSPINI VESLAQVKMH FQKLRFEGWA EKTSDSTTIK NDGKTVAIDV GGDFFVSGGG
LRSKFKVGRI TFHWGLCNAS SDGSEHGLND EKFPLEMQIY CYEADVFGSL DEALRAGGKI
TALAVLFDIN TVDNENYMAI IDAVNSVSRY GKSGPVSPFT LQGVLPNSTE KYFIYNGSLT
TPPCSETVEW IVFKNRVTIS DVQLEMFCEV MTMQQAGYVM LMDYLQNNYR EQQEQFMGQV
FSSYTGVEEV HTPICSSEPE NVQANPHNHT SMLVIWERPR AVYDASIERY SVTYRPSQGD
DESALEYLTD GDQDVGAIIQ DLLANTSYMV QVVAVCTNGL YGRVSDQLTV DMPLDDPEAD
NDSDSFEYDE EEDYHINPFL IRPGTNQLPY PFQTTTTSPR VTTTQRPVHP VFKTTPRTHE
QRFPVEDSQK THDHYIPVIS TDKPTVKYTD KPTIPTTRAT ILAIDVHTTR PDGSHIVAGV
SSESDGQSNT FTDSPTSVTP ETRVIPKTRV IPETRVIPET SITPDTRVIP EISVTSETSI
APETKVIPEI SVTSETRVIP EISVTSETRV IPEISVTSET RVIPEISVTP ETKVIPEISI
TSETRVIPEI SVTPETRVIP EISIDPETRV TPEISVIPET SVTPETSITP ETSGTPETRV
IPEISVIPET SVTPEISRTL ETSVTLETSI TLKTDVISPS IDISEVEEVT QPITDSHSYG
KSPVTVAPLF EIPMESTSST FPPEVPLWPT TASLPFPTTA AFSTVLLQTT QPVFNGESAS
YVPSVSDTLS YVHASPVSPY SLSSVLSEPI PDWDIPYTVS MQVYGGAQSI TPSPSYPTLL
LTGSVSFLDM EPVSSGGCND DDGDDDNLSG SISADPQCRS TLPLPTLPKV AASVVSIQSS
SEHDLSESPS IVSTLSTLAY LQPSVPVSLM TTNLDSDASP SGSVGDSRLL TEWVDYSLVA
PTYSQDSGAS TEISLHASSN FLLPSSTSGL PPCSGLLGDL SSPVEHHLFL STSSAGTLLC
RDTDLDLHTE ALLSTPPIST MPSSDLSISI SANVSSVPQS ATGQSQGAPA PVRSASIAPT
STPEFIFIPT PVVPPTVAPT SPPESISVVA PVVPPTVAVL SVPEFSSIPT HSADGQLENS
ASGWALDLDW GQSSASGDES IVPYITTATP TEVAPEEMDD GNEEHSSSFY FEGENGTESE
APDFRVTLRP SPSWTLRGSG EEESGSGENL TDNETSSDFS IPERTERDSE EEPVEDAGNS
SHESRVGLAS SIERQKKAVI PLAVVSTLTF LGLIVLIGIF IYWRHVFTLP GEHEPQSVKQ
FVKHVAALHN TNSFSREFEI LKEYFEEVQT CTVDLGTTTD CSSHPDNKNK NRYVNILAYD
HSRVRLAPLN DKDGRSGGDY INANYVDPYL SLLSVSHKGF NKQKAYIAAQ GPLKSSTVDF
WRMVWEQNVG VIVMITNLVE KGRRKCDQYW PLENQEEYGC FLVTVKSTNV LAYYTQRTFT
IRNTSIKKRA RSNERTVIHY HYTQWPDMGV PEYVLPVLSF IYKSSRAQTE HMGSMIVHCS
AGVGRTGTYI VLDSMLKQIK VQGTVNIVGF LKHIRTQRNY LVQTEEQYVF THDALVEAIL
SQETEVPTSH IHQYVNNLLT PGASCKTRLE KQFKLVCQSN AKQKDYSSAL NDCNRMKNRS
CSLIPVEKSR VCLSTSAGET SDYINASYVM GYRQSKEFII TQNPLPSTVK DLWRMVWDHN
SQVIISLLDT SSTTKDNEPI TFWPVRDQPI IYETFSVSLR GEGHVCLSNE DILIVQDYIL
EASQDDFVLE VKHYRAPRWP NPDSPISSVF ELINIIQKEF SSKDGPMVVH DEHGGVTAGT
FCALFTLLQQ LEAESAVNVY MVAKMINLMR PGVFTDIDQY QFLYKAILSL VSTQEDERAL
QSSDNNGTVP GGVSSAAESL ESLV
//
