ID A0A3Q1JJP2_ANATE Unreviewed; 1937 AA.
AC A0A3Q1JJP2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
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};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000030979.2, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000030979.2}
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 -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 2A subfamily. {ECO:0000256|ARBA:ARBA00010504}.
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DR Ensembl; ENSATET00000031442.2; ENSATEP00000030979.2; ENSATEG00000021335.2.
DR GeneTree; ENSGT00940000153617; -.
DR Proteomes; UP000265040; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd00063; FN3; 8.
DR CDD; cd05738; IgI_2_RPTP_IIa_LAR_like; 1.
DR CDD; cd05739; IgI_3_RPTP_IIa_LAR_like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 11.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
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; PTHR46957; CYTOKINE RECEPTOR; 1.
DR PANTHER; PTHR46957:SF8; PROTEIN TYROSINE PHOSPHATASE RECEPTOR TYPE S; 1.
DR Pfam; PF00041; fn3; 7.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF13927; Ig_3; 1.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00014; FNTYPEIII.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 8.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SMART; SM00194; PTPc; 2.
DR SMART; SM00404; PTPc_motif; 2.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR SUPFAM; SSF49265; Fibronectin type III; 5.
DR SUPFAM; SSF48726; Immunoglobulin; 3.
DR PROSITE; PS50853; FN3; 8.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 2.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000265040};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1937
FT /note="protein-tyrosine-phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030080467"
FT TRANSMEM 1274..1297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 31..121
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 133..225
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 237..319
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 326..416
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 421..517
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 519..612
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 617..713
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 718..826
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 827..921
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 925..1020
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1024..1108
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1382..1637
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1557..1628
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1669..1928
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1846..1919
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 1308..1327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1937 AA; 216442 MW; BD3EA7CA8ABC8128 CRC64;
MHVSTYPTMH SASPGLLLLS FLFLADADSP PRFTRTPEDQ TGVQGGVASF VCQAAGDPQP
KIVWNKKGKK VSNQRFEVIE FDDGSGSVLR IQPLRTPRDE AIYECHASNS AGEITASTRL
NVLREDQLPS GFPTIDMGPQ LKVVERSRTA TMLCAASGNP DPEITWFKDF LPVNTSNNNG
RIKQLRSESF GALQIEMSEE SDQGKYECVA TNSDGTRYST PANLYVRELR EVRRVPPRFS
IPPADSEIMP GGNVNITCVA VGSPMPYVKW MLGAEDLTPE DDMPIGRNVL ELTDVRQSNN
YTCVAMSTLG VIEAVAQIIV KALPKAPGTP VVTERTATSI TLTWDSGNPE PVSYYIIQHR
AKGSEDPYKE IDGIATTRYS VGGLSPYSHY DFRVAAVNTI GQGPSSDVVE ARTAEQAPSS
PPRQVRGRML STTTAIIHWD EPEEPNGQVV GYRVYYTSDN TLPVNQWEKQ MVRSANFITI
QGLTPNKTYY IRVLAFTSVG DGPLSQDLQI IAKTGVPSQP SEFKGEAKSE TSILLTWVAP
PQGGPDNQIT GYELVYRRAD DTEEKKVSFE PSTSYLLKNL KPFSTYTFQL AARSKHGIGA
YTNEVSIDTP QTLPSAPPQD ITCTSPSSTS ILVSWTPPPL EFQNGIITGY SIQYSNTEGN
KTSKRIDGIP PESSPYLLEN LEKWTEYGIT IRAQTEAGDG PESLQLLIRT EEDVPSGPPR
GVEAETVNAS AIRVKWRAPA PERQHGQIRG YQVHYVRMNY GEPQGQPFIK DILIEDSQWA
HDDSAEYEVV LGDLKADTSY SVSVGAYTAK GDGARSKPVT VCTALPLPEK PKLVVSATDS
GTALLQWYPP PNPPTPLLGY RLTFGRIDVL PYTVVEFPTK ENRYTAHDIH KGANYVFRIS
ARNKMGYGEE AVKEVSTPED APSGFPENII CEEASATSLQ LEWKSVPLIE QNGKITKYSV
LYKDINSRGN ASEVVVPAPG LSVLLEGLSA DTVYDVRVSA FTAVGAGPYS PSAQFRTQRL
DQVFATNFRV KAAMKNSILL SWEIRDKNPA QPFTILYGKG QSVEVDGKHT QKLISGLEPD
TQYSFLLTNR ANSAGGLQHR VTATTAPDIL KTKPMVVGKT NADGMVTVQL PTVQTTAKVR
GYYVVVVPLK KQKGKFLNPW EEPDQMNLDE LLKEINRTSV SHALRIRRQA AQSDPRAYVT
AHFKTLPLEF TLGDGRNYGD FRNRPLQNGQ EYVFFVLAML DLSENTMYAT SPYSDPVTSS
DVDPQPMVDE EEGLLWVVGP VLAVIFIVCI VIAILLFKSK PDRKRAEAEG RKGSFPCSKA
MSSHHPTDPV ELRRINFQTP AYRVSVYRGY RRLSSMASHP PVPMSELADH IERLKANDNL
KFSQEYESID PGQQFTWENS NLEVNKPKNR YANVIAYDHS RVILSSIEGV PGSDYINANY
IDGYRRQNAY IATQGSLPET FGDFWRMVWE QHTANIIMMT KLEEKSRVKC DQYWPTRGTE
TYGLIQVTLL DTVELATYSV RTFALYKSGS NEKREVRHFQ FTAWPDHGVP EHPTPFLAFL
RRVKACNPPD AGPMVVHCSA GVGRTGCFIV IDAMTERIKH EKTIDIYGHV TLMRSQRNYM
VQTEDQYIFI HDALLEAVTC GNTEVPARNL YSYIQRLTQI EPGENVTGME LEFKRLASAK
AHTSRFVSAN LPCNKFKNRL VNIMPYETTR VCLQPIRGVE GSDYINASFI DGYRQQKAYI
ATQGPLAETT EDYWRMLWEH NSTIVVMLTK LREMGREKCH QYWPAERSAR YQYFVVDPMA
EYNMPQYILR EFKVTDARDG QSRTVRQFQF TDWPEQGVPK SGEGFIDFIG QVHKTKEQFG
QDGPITVHCS AGVGRTGVFI TLSIVLERMR YEGVVDIFQT VKMLRTQRPA TVQTEDQYQF
CYRASLEYLG SFDHYAT
//
