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Database: UniProt
Entry: A0A3B4URN9_SERDU
LinkDB: A0A3B4URN9_SERDU
Original site: A0A3B4URN9_SERDU 
ID   A0A3B4URN9_SERDU        Unreviewed;       833 AA.
AC   A0A3B4URN9;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Protein tyrosine phosphatase receptor type N {ECO:0000313|Ensembl:ENSSDUP00000020440.1};
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:ENSSDUP00000020440.1, ECO:0000313|Proteomes:UP000261420};
RN   [1] {ECO:0000313|Ensembl:ENSSDUP00000020440.1}
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; A0A3B4URN9; -.
DR   STRING; 41447.ENSSDUP00000020440; -.
DR   Ensembl; ENSSDUT00000020809.1; ENSSDUP00000020440.1; ENSSDUG00000014837.1.
DR   GeneTree; ENSGT00940000154095; -.
DR   OMA; AQTGFQI; -.
DR   Proteomes; UP000261420; 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          563..823
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          742..814
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          67..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          262..325
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          497..539
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        268..282
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        501..539
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   833 AA;  91870 MW;  9D4657C6E63F5C20 CRC64;
     CTRDQFCSDD GLFGQCLSSK QDQVQYQVSV PVLKRMQEVL KQLMLQGLSW QDDITQYILS
     KELKRVPHTT HPSKSKQHVP HHHSSKSGST PSAGNYVDYM IVEPPQSQLR CVSAAQVYAR
     PSSRSQASQR ERERDRQLLQ EALSLYLASA QPSYRHRGAA SMAPAGLPYY DDLELDIPMD
     YVEGYTLEER LGTAGRQQML QNKKVPQDYS TLSGNNDGLL QRMSGVLQRY GVDPRELSQE
     QLYKLALILQ LLQMQLLKTD SVSNKPQKPV PVPGPPDAPL APSSASIPAT PAAKSASPPP
     SATQPPQAAP AEAGQGLKEQ GPPLVEGMGA KEEYGYIVTN QSPLGLYDGV KLLELLADKI
     HLTTSSFINI SVVGPALTFR IRQNEHNMTA AEVAAKAVSE KNFLESQTGL KIVQTGVGER
     TDARGLPQVT RVSQGSSGTV ITLVSMAVVG GVLVLAMAVA CLRHYAQQVA NGKLGLGPEG
     GAETHFDYQD CVATGAGGRR GTDTSRVSSV SSQFSDGPQH SPSSTHSSTP SWSEEPAQSN
     MDISTGHMIL AYMEDHLRNK DRLQKEWEAL CSYQAEPSSV AAAQVPSNMD KNRNAESLPY
     DHTRVKLKTE LNPNKQDYIN ASIIFDHDPR QPAYIATQGP LSHTVADFWQ MVWENGCTVI
     VMMSALVEDG EKQCERYWPD EGSSLYHIYE VNLVSEHIWC KDFLVRSFYL KNVQTQETRT
     LTQFHLLSWP ADGIPTSTRP LLDFRRKVNK CYRGRSCPII VHCSDGTSRT GTYILIDMVL
     NRMAKGVKEI DIAAALEHIR DQRPGLVRTK DQFEFALTAV AEEVNAILKA LPQ
//
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