ID A0A2Y9IXT6_ENHLU Unreviewed; 979 AA.
AC A0A2Y9IXT6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Receptor-type tyrosine-protein phosphatase-like N isoform X1 {ECO:0000313|RefSeq:XP_022353422.1};
GN Name=LOC111143810 {ECO:0000313|RefSeq:XP_022353422.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022353422.1};
RN [1] {ECO:0000313|RefSeq:XP_022353422.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022353422.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane
CC {ECO:0000256|ARBA:ARBA00004212}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004212}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 8 subfamily. {ECO:0000256|ARBA:ARBA00025723}.
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DR RefSeq; XP_022353422.1; XM_022497714.1.
DR AlphaFoldDB; A0A2Y9IXT6; -.
DR STRING; 391180.A0A2Y9IXT6; -.
DR KEGG; elk:111143810; -.
DR OrthoDB; 2911650at2759; -.
DR Proteomes; UP000248482; Unplaced.
DR GO; GO:0030141; C:secretory granule; IEA:InterPro.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-KW.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd14609; R-PTP-N; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR Gene3D; 3.30.70.2470; Protein-tyrosine phosphatase receptor IA-2 ectodomain; 1.
DR InterPro; IPR033522; IA-2/IA-2_beta.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR021613; Receptor_IA-2_dom.
DR InterPro; IPR038112; Receptor_IA-2_ectodomain_sf.
DR InterPro; IPR029403; RESP18_dom.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR PANTHER; PTHR46106; IA-2 PROTEIN TYROSINE PHOSPHATASE, ISOFORM C; 1.
DR PANTHER; PTHR46106:SF1; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE-LIKE N; 1.
DR Pfam; PF11548; Receptor_IA-2; 1.
DR Pfam; PF14948; RESP18; 1.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SMART; SM01305; RESP18; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 3: Inferred from homology;
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000313|RefSeq:XP_022353422.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW Signal {ECO:0000256|SAM:SignalP}; Synapse {ECO:0000256|ARBA:ARBA00023018};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..979
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015866515"
FT TRANSMEM 577..600
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 709..969
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 888..960
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 112..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..680
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 979 AA; 106100 MW; B6C6113CE7C586AB CRC64;
MRRPRRPGGP GGSGGLRVLL CLLLLSSRPG GCSAISAHGC LFDRRLCSHL EVCIQDGLFG
QCQVGVGQAR PLLQVTSPVL QRLQSVLRQL MSQGLSWHDD LTQYVISQEM ERIPRLHPPE
PRPRDRSGLV PRRPGPAGEL LLQGIPTGST PAAQHRLPQP PGGGGGTGVG SPLSPLQAEL
LPPLLEHLLL PPQAPHPALS YEPALLQPYL FHQFGSRDGS RGSEGSPGMV SVGPLPKAEP
STLFSRTASK DLFGAHSDHS YGDPPGPSPG QLFQDSGLLY LAQELPVPSR ARAPRLPEQG
GSSRAKDSSE GYEEEGLEGR REKPSSPAEQ PDVTLQRLAA VLAGYGVELR QLTPEQLSTL
STLLQLLPKG AGRNLGGVVN VGADIKKTTE EQVQGENTVE PPPPTPSLPE YHTASPTSNK
AQQVLSSGSS ESPEAATQLA TPVLLEKKSP LSQSQSPTAR QPSAQPSAEE YGYIVTDQKP
LSLAAGVKLL EILAEHVHVS SGSFINISVV GPALTFRIRH NEQNLSLADV THQAGLVKSE
LEAQTGLQIL QTGVGQREEA AAVLPRPARS TSPMRSVLLT LVALAGVAGL LVALAVALCV
RQHARQRDKE RLAALGPEGA HGDTTFEYQD LCRQHMATKS LFSRAEGPPE PSRVSSVSSQ
FSDAAQASPS SHSSTPSWCE EPAQANMDIS TGHMILAYME DHLRNRDRLA KEWQALCAYQ
AEPNTCAAAQ GEGNIKKNRH PDFLPYDHAR IKLKVESSPS RSDYINASPI IEHDPRMPAY
IATQGPLSHT IADFWQMVWE SGCTAIVMLT PLVEDGVKQC DRYWPDEGSS LYHVYEVNLV
SEHIWCEDFL VRSFYLKNVQ TQETRTLTQF HFLSWPAEGT PASTRPLLDF RRKVNKCYRG
RSCPIIVHCS DGAGRTGTYI LIDMVLNRMA KGVKEIDIAA TLEHVRDQRP GLVRSKDQFE
FALTAVAEEV NAILKALPQ
//
