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Database: UniProt
Entry: A0A3B4X5Y9_SERLL
LinkDB: A0A3B4X5Y9_SERLL
Original site: A0A3B4X5Y9_SERLL 
ID   A0A3B4X5Y9_SERLL        Unreviewed;       857 AA.
AC   A0A3B4X5Y9;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Receptor-type tyrosine-protein phosphatase-like N {ECO:0000313|Ensembl:ENSSLDP00000011556.1};
OS   Seriola lalandi dorsalis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000011556.1, ECO:0000313|Proteomes:UP000261360};
RN   [1] {ECO:0000313|Ensembl:ENSSLDP00000011556.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   AlphaFoldDB; A0A3B4X5Y9; -.
DR   STRING; 1841481.ENSSLDP00000011556; -.
DR   Ensembl; ENSSLDT00000011969.1; ENSSLDP00000011556.1; ENSSLDG00000009077.1.
DR   GeneTree; ENSGT00940000154095; -.
DR   Proteomes; UP000261360; 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   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   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT   DOMAIN          587..847
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          766..838
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          65..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          138..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          286..349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          521..563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..95
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..306
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        525..563
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   857 AA;  94614 MW;  89A2BF57E13FEA4F CRC64;
     TRDQFCSDDG LFGQCLSSKQ DQVQYQVSVP VLKRMQEVLK QLMLQGLSWQ DDITQYILSK
     ELKRVPHTTH PPKPNFSSSS SHPPHSKSGS TPSAGNYVDY MIVEPPQSQL RMQTASMDPY
     TYHQHRYQDE VERSLLGAGG SYARPSSRSQ ANQRERERDR QLLQEALSLY LASAQPSYRH
     RGAASMAPAG LPYYDDLELD IPIDYVEGYN LEERLGTAGR QQMLQNKKVP QDYSTLSGNN
     DGLLQRMSGV LQRYGVDPRE LSQEQLYKLA LILQLLQMQL LKTDSVSNKP QKPVPVPGPP
     DAPLAPSSAS IPATPAAKSS SPPPSATQPP QAAPAEAGQG LKEQGPPLVE GMGAKEEYGY
     IVTNQSPLGL YDGVKLLELL ADKIHLTTSS FINISVVGPA LTFRIRQNEH NMTAAEVAAK
     AVSEKNFLES QTGLKIVQTG VGERTDARGL PQVTRVSQGS SGTVITLVSM AVVGGVLVLA
     MAVACLRHYA QQVANGKLGL GPEGGAETHF DYQDCVATGA GGRRGTDTSR VSSVSSQFSD
     GPQHSPSSTH SSTPSWSEEP AQSNMDISTG HMILAYMEDH LRNKDRLQKE WEALCSYQAE
     PSSVAAAQVP SNMDKNRNAE SLPYDHTRVK LKTDLNPNKQ DYINASIICD HDPRQPAYIA
     TQGPMSHTVA DFWQMVWENG CTVIVMMSAL VEDGEKQCER YWPDEGSSLY HIYEVNLVSE
     HIWCKDFLVR SFYLKNVQTQ ETRTLTQFHL LSWPADGIPT STRPLLDFRR KVNKCYRGRS
     CPIIVHCSDG TSRTGTYILI DMVLNRMAKG VKEIDIAAAL EHIRDQRPGL VRTKDQFEFA
     LTAVAEEVNA ILKALPQ
//
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