ID A0A3B4UIG5_SERDU Unreviewed; 1406 AA.
AC A0A3B4UIG5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000018033.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000018033.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 Ensembl; ENSSDUT00000018361.1; ENSSDUP00000018033.1; ENSSDUG00000013071.1.
DR GeneTree; ENSGT00940000157151; -.
DR OMA; WLLFRTH; -.
DR Proteomes; UP000261420; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
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; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
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; 2.
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; SM00409; IG; 1.
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; PS50835; IG_LIKE; 1.
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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 720..743
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 9..171
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 173..262
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 269..364
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 367..468
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 474..575
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 873..1104
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1024..1095
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1136..1399
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1315..1390
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 797..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..812
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1406 AA; 158143 MW; B20F960BCDFF20BE CRC64;
MFSFFFPAAG CTFEEDSDPN LCDFTQGEED DFDWLLFRTY SSPYASSDLL RGSYMLVNSS
QHAVGHRAQL LLQSLSENDT HCVQFSYFLY SRDGHSPGAL RAYVRVNGGP LGSPVWNTSG
SHAKQWHQVE LAVSTFWPNE YQVLIEATVS RERRGYIAID DIMVLNYPCY KAPHFSRLGD
EEVNAGQNAT FQCVAAGRAS EAEKFLLEVS GLMVAKGTCH LSHRRFVVSF QLDSVQRSDQ
DLYRCVTQSP RGSGVSNFAE LVVKVPPSPI APPQLLRAGS TYLIIQLNTN SILGDGPIIR
KEIEYRASQS PWSEVHGVNM VTYKLWHLDP DTEYHISVLL TRPGEGGTGP PGPPLVSRTK
CAEPMRALRG LTATDIQSRQ LSLQWENLAF NLTRCHTYSV SLCYRYTTAG GGGGHNTTVR
ECLAVEHNAS RFTLRDLPPY HGIHVRLSLA NPEGKKEGRE VTFQTEEDIP GGIAPESLTF
TPLDDMIFLK WEEPVEPNGL ITQYEISYQS IESSDPGINV PGPRRTVSKL KNETYHMFSN
LHPGTTYLIS VRARTAKGFG QTALTEITTN ISAPTFDYGD MPSPLSETES TITVLLRPAQ
GRGAPVSTYQ VVVEEETVKK VKRELGLQEC FPLPMSHGEA QARGTPHYYT AELPPSSLPE
ASPFTVGDNH TYNGYWNSPL DPRKSYLVYF QAMSNFRGVT ACKDHRKALE VSQHSEEMGL
ILGVCAGGLV VLILLLGAVI IIIKKGKPVN MNKTPITYRQ EKSHMGSMER SFTDQSTLQE
DERMALSFMD AHTCGTRSDA RSSVNEASSL LGGSPRHQCG RKGSPYHTGQ LHPAVRVADL
LQHINQMKTA EGYGFKQEYE SFFDGWDCTK KKDKTKGRHD TLLGYDRHRV KLHPLLGDPN
SDYINANYID GYHRSNHFIA TQGPKQETLY DFWRMVWQEN CFSIVMITKL VEVGRVKCCK
YWPDDSEMYG DIKITLLKTE TLAEYTVRTF ALERRGYSTK HEVRQFHFTS WPEHGVPYHA
TGLLSFIRRV KASTPPDAGP VVVHCSVGAG RTGCYIVLDV MLDMAECEGV VDIYNCVKTL
CSRRINMIQT EEQYIFIHDA ILEACLCGET AILVNEFAVT YKEMLRVDSQ SNSSQLREEF
QTLNSVTPHL DVEECSIALL PRNREKNRSM DVLPPDRALA FLVTTEGESN NYINAALADS
FHRQAAFIVT PHPLPGTTAD FWRLVFDYGC TAVVMLNQLN QSNSAWPCVQ YWPEPGLQQY
GPMEVEFLSM SADEDVITRL FRVKNVTRLQ EGQLVVCQFQ FLRWSAYRDV PDSKKAFLNL
LAQVHKWQRE CGEGRTAVHC LNGGGRSGTF CACNILLEMI QYQNMVDIFY AVKTLRNCKP
NMVESLDQYR FCYDLVLEYL DCFEGR
//
