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Database: UniProt
Entry: A0A2Y9G474_TRIMA
LinkDB: A0A2Y9G474_TRIMA
Original site: A0A2Y9G474_TRIMA 
ID   A0A2Y9G474_TRIMA        Unreviewed;      1239 AA.
AC   A0A2Y9G474;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Receptor-type tyrosine-protein phosphatase T {ECO:0000313|RefSeq:XP_012414133.1};
GN   Name=LOC101353284 {ECO:0000313|RefSeq:XP_012414133.1};
OS   Trichechus manatus latirostris (Florida manatee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX   NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_012414133.1};
RN   [1] {ECO:0000313|RefSeq:XP_012414133.1}
RP   IDENTIFICATION.
RG   RefSeq;
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   RefSeq; XP_012414133.1; XM_012558679.1.
DR   AlphaFoldDB; A0A2Y9G474; -.
DR   STRING; 127582.A0A2Y9G474; -.
DR   GeneID; 101353284; -.
DR   KEGG; tmu:101353284; -.
DR   InParanoid; A0A2Y9G474; -.
DR   OrthoDB; 2875525at2759; -.
DR   Proteomes; UP000248480; 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; 3.
DR   CDD; cd06263; MAM; 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; 4.
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; IPR000998; MAM_dom.
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; PTHR24051:SF8; PROTEIN-TYROSINE-PHOSPHATASE; 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; 4.
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; 1.
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; 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   Receptor {ECO:0000256|ARBA:ARBA00023170,
KW   ECO:0000313|RefSeq:XP_012414133.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248480};
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        627..648
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          4..165
FT                   /note="MAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50060"
FT   DOMAIN          167..258
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          265..358
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          363..457
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          460..563
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          769..990
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          908..981
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          1022..1239
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1195..1239
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          670..707
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1239
FT                   /evidence="ECO:0000313|RefSeq:XP_012414133.1"
SQ   SEQUENCE   1239 AA;  138992 MW;  4AF5DA8F03942359 CRC64;
     MFTGGCSFDE HYSNCGYSVA LGTNGFTWEQ INTWEKPMLD PAVPTGSFMM VNSSGRASGQ
     KAHLLLPTLK ENDTHCIDFH YYFSSRDRSS PGALNVYVKV NGGPQGNPVW NVSGVVTEGW
     VKAELAISTF WPHFYQVIFE SVSLKGHPGY IAVDEVRVLA HPCRKAPHFL RLQNVEVNVG
     QNATFQCIAG GKWSQHDKLW LQQWNGRDTA LMVTRVVNHR RFSATVSVAD TAQRSVSKYR
     CVIRSDGGSG VSNYAELIVK EPPTPIAPPE LLAVGATYLW IKPNANSIIG DGPIILKEVE
     YRTTTGTWAE THIVDSPNYK LWHLDPDVEY EIRVLLTRPG EGGTGPPGPP LTTRTKCADP
     VHGPQNVEIV DIRARQLTLQ WEPFGYAVTR CHSYNLTVRY QYVFNQQQYE AEEVIQTSSH
     YTLRGLRPFM TIRLRLLLSN PEGRMESEEL VVQTEEDVNQ AMALELQKPK FESQIFISWG
     PVNESNGVVR YFKINYKAVG SLDPSADLSS QRGKVFKLRN ETHHLFVGLY PGTTYSFTIK
     ASTAKGFGPP VTTRIATKIS APSMPEYDTD TPLNETDTTI TVMLKPAQSR GAPETKINCV
     RLATKGASTQ NSNTVEPEKQ VDNTVKMAGV IAGLLMFIII LLGVMLTIKR RRNAYSYSYY
     LKLAKKQKET QSGAQREMGP VASADKPTAK LSANRNDEGF SSSSQDVNGF TDGSRGELSQ
     PTLTIQTHPY LTCDPMEMSY PRDQFQPAIR VADLLQHITQ MKRGQGYGFK EEYEALPEGQ
     TASWDTAKED ENRNKNRYGN IISYDHSRVR LLVLDGDPHS DYINANYIDG YHRPRHYIAT
     QGPMQETVKD FWRMIWQENS ASIVMVTNLV EVGRVKCVRY WPDDTEVYGD IKVTLIETEP
     LAEYVIRTFT VQKVKLFGNP HQAGPIAAHC SNAGAGRTGC FIAIDTMLDM AENEGVVDIF
     NCVRELRAQR VNLVQTEEQY VFVHDAILEA CLCGNTAIPV CEFRSLYYNI SRLDPQTNSS
     QIKDEFQTLN IVTPRVRPED CSIGLLPRNH DKNRNMDVLP LDRCLPFLIS VDGESSNYIN
     AALMDSHKQP AAFVVTQHPL PNTVADFWRL VFDYNCSSVV MLNEMDTAQL CMQYWPEKTS
     GCYGPIQVEF VSADIDEDII HRIFRICNMA RGTSSRYCSC GFRINVSSNL ESLNGGGRSG
     TFCAICSVCE MIQQQNIIDV FHIVKTLRNN KSNMVETLV
//
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