ID W5M769_LEPOC Unreviewed; 1485 AA.
AC W5M769;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000004227.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000004227.1}
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 -!- 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 2B subfamily. {ECO:0000256|ARBA:ARBA00006396}.
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DR EMBL; AHAT01009521; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 7918.ENSLOCP00000004227; -.
DR Ensembl; ENSLOCT00000004235.1; ENSLOCP00000004227.1; ENSLOCG00000003524.1.
DR eggNOG; KOG4228; Eukaryota.
DR GeneTree; ENSGT00940000157151; -.
DR HOGENOM; CLU_001645_0_0_1; -.
DR InParanoid; W5M769; -.
DR OMA; RICMYLE; -.
DR Proteomes; UP000018468; Linkage group LG6.
DR Bgee; ENSLOCG00000003524; Expressed in camera-type eye and 13 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd00063; FN3; 2.
DR CDD; cd06263; MAM; 1.
DR CDD; cd14632; R-PTPc-U-1; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR000998; MAM_dom.
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; PTHR24051:SF10; PROTEIN-TYROSINE-PHOSPHATASE-RELATED; 1.
DR PANTHER; PTHR24051; SUSHI DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00629; MAM; 1.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00020; MAMDOMAIN.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00137; MAM; 1.
DR SMART; SM00194; PTPc; 2.
DR SMART; SM00404; PTPc_motif; 2.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS00740; MAM_1; 1.
DR PROSITE; PS50060; MAM_2; 1.
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:UP000018468};
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..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1485
FT /note="protein-tyrosine-phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004865650"
FT TRANSMEM 747..770
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1464..1483
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 24..186
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 286..381
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 384..484
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 485..590
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 911..1148
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1068..1139
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1180..1443
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1359..1434
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 831..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..852
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1485 AA; 168010 MW; 52DD0CB11825B4CA CRC64;
MNTLAFLLIL AVRIYADGSE APTGGCTFDE DSDPSLCEYS QGEEDDFDWQ LMRTYSSPHS
TSDLLYGSYM MVNSSEHAEG QRAHLLLQTL SENDTHCVQF SYFLYSRDGH SPGDLKAYVR
VNAGPLGSPV WNVSGSHGRQ WHQVELAVST FWPNEYQVLF EATISKERRG YIGMDDILLL
NYPCYKAPHF SRLGDVEVNA GQNATFQCVA SGRASETERF LLERHNGDVT LASSVKHLSH
RRFLASFQLD MVQRGGQDLY RCVTQSSRGS GVSNFAELIV KVPPSPIAPP QLLRAGSTYL
IIQLNTNSIL GDGPIIRREI EYRASQAPWS EVHGVNMATY KLWHLDPDTE YHISVLLTRP
GEGGTGPPGP PLISRTKCAE PMRALRALTA TEIQSRQLSL QWEPLGYNLT RCHTYSVSLC
YRYAGGSGAG HNTTVRECLA VEHNASRFVL RDLPPYRTVH VRLALSNPEG KKESREVAFQ
TEEDIPGGIA SESLTFTPLE DMIFLKWEEP VEPNGLITQY EISYQSIESS DPGINVPGPR
RTVSKLRNET YHMFSNLHPG TTYLISVRAR TGKGFGQTAL TEITTNISAP MFDYGDMPPP
LGESESTITV LLRPAQGRGA PVSTYQVVVE EDRPKKVKRD LGNVECFPIP TTHSEAQARG
TLHYYTAELP PSSLPTATPF TVGDNQTYRG YWNSPLDPRK NYLIYFQAMS NFRGETRINC
IRIARKAACK DAKRALEVTQ HSEEMGLILG VCAGGLVVLI LLMGAIIIII KKGRDYYSYS
YYPKPVNINK TPITYRQEKT HMIGSMDRSF TDQSTLQEDE RMALSFMDAH NCSSRSDQRS
SVNESSSLLG GSPRRQCGRK GSPYHTGQLH PAVRVADLLQ HINQMKTAEG YGFKQEYESF
FEGWDVSKKK DKTKGRHESL LGYDRHRVKL HPLLGDPNSE YINANYIDIR INREGYHRSN
HFIATQGPKQ ETVYDFWRMV WQENCFSIVM ITKLVEVGRV KCCKYWPDDS DMYGDIKITL
MKTETLAEYT VRTFTLERRG YSAKHEVRQF HFTSWPEHGV PYHATGLLAF IRRVKASTPP
DAGPVVVHCS VGAGRTGCYI VLDVMLDMAE CEGVVDIYNC VKTLCSRRIN MIQTEEQYIF
IHDAILEACL CGETAIPVRE FSLTYKEMLR VDSQSNSSQL REEFQTLNSV TPHLDVEECS
IALLPRNREK NRSMDVLPPD RCLPFLITTE GESNNYVNAA LTDSFLRSAA FIVTPHPLPG
TTTDFWRLVF DYGCTSLVML NQLNQSNSAW PCVQYWPEPG LQQYGPMQVE FLSRSSDEDV
ITRLFRVKNV TRLQEGHLMV RQFQYLRWSA YREVPDSKKS FLNLLGHVHK WQRECGEGRT
IVHCLNGGGR SGTFCACTTL LEMMQYQSMV DVFYAVKTLR NSKPNMVESL EQYRFCYDLA
LEYLECMESC PESCQRSISN LNNFLVLCTV HVFVVLQWTR LLFSA
//
