GenomeNet

Database: UniProt
Entry: M3YYW0_MUSPF
LinkDB: M3YYW0_MUSPF
Original site: M3YYW0_MUSPF 
ID   M3YYW0_MUSPF            Unreviewed;       979 AA.
AC   M3YYW0;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   SubName: Full=Protein tyrosine phosphatase receptor type N {ECO:0000313|Ensembl:ENSMPUP00000016520.1};
DE   SubName: Full=Receptor-type tyrosine-protein phosphatase-like N isoform X2 {ECO:0000313|RefSeq:XP_004762895.1};
GN   Name=PTPRN {ECO:0000313|Ensembl:ENSMPUP00000016520.1,
GN   ECO:0000313|RefSeq:XP_004762895.1};
OS   Mustela putorius furo (European domestic ferret) (Mustela furo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Mustelinae; Mustela.
OX   NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000016520.1};
RN   [1] {ECO:0000313|Ensembl:ENSMPUP00000016520.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2023) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_004762895.1}
RP   IDENTIFICATION.
RC   TISSUE=Brain {ECO:0000313|RefSeq:XP_004762895.1};
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   EMBL; AEYP01056839; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_004762895.1; XM_004762838.3.
DR   STRING; 9669.ENSMPUP00000016520; -.
DR   Ensembl; ENSMPUT00000016766.1; ENSMPUP00000016520.1; ENSMPUG00000016623.1.
DR   GeneID; 101679207; -.
DR   KEGG; mpuf:101679207; -.
DR   CTD; 5798; -.
DR   eggNOG; KOG0793; Eukaryota.
DR   GeneTree; ENSGT00940000154095; -.
DR   HOGENOM; CLU_007905_2_0_1; -.
DR   OMA; AQTGFQI; -.
DR   OrthoDB; 2911650at2759; -.
DR   Proteomes; UP000000715; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
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:0030507; F:spectrin binding; IEA:Ensembl.
DR   GO; GO:0044389; F:ubiquitin-like protein ligase binding; IEA:Ensembl.
DR   GO; GO:1990502; P:dense core granule maturation; IEA:Ensembl.
DR   GO; GO:0030073; P:insulin secretion; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:1904692; P:positive regulation of type B pancreatic cell proliferation; IEA:Ensembl.
DR   GO; GO:0000302; P:response to reactive oxygen species; IEA:Ensembl.
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_004762895.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000715};
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_5041118249"
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..242
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          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        399..413
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        414..437
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;  105986 MW;  401E2F5558126BB5 CRC64;
     MRRPRRPGGP GGSGGLRVLL CLLLLSSRPG GCSAISAHGC LFDRRLCSHL EVCIQDGLFG
     QCQVGVGQAR PLLQVTSPVL QRLQSVLRQL MSQGLSWHDD LTQYVISQEM ERIPRLHPPE
     PRPRDRSGLV PRRPGPAGEL LLQGIPTGST PAAQHRLPQP PGGGGGAGVG SPLSPLQAEL
     LPPLLEHLLL PPQAPHPALS YEPALLQPYL FHQFGSRDGS RGSEGSPGMV SVGPLPKAES
     STLLSRTASK DLFGAHSDHS YGDPPGPSPG QLFQDSGLLY LAQELPVPSR ARAPRLPEQG
     GSSRAKDSSE GYEEEGQEGR REKPSSPAEQ PDVTLQRLAA VLAGYGVELR QLIPEQLSTL
     STLLQLLPKG AGRNLGAVVN VGADIKKTTE EQVQGENTVE PPPPTPSLPE YPTASPTPNK
     AQQVLSSGSS ESPKAATQLA TPVLLEKKSP LGQSQPPAAR QPSAQPSAEE YGYIVTDQKP
     LSLAAGVKLL EILAEHVHVS SGSFINISVV GPALTFRIRH NEQNLSLADV THQAGLVKSE
     LEAQTGLQIL QTGVGQREEA AAVLPRPARS TSPMRSVLLT VVALAGVAGL LVALAVALCV
     RQHARQRDKE RLAALGPEGA HGDTTFEYQD LCRQHMATKS LFSRAEGPPE PSRVSSVSSQ
     FSDAAQASPS SHSSTPSWCE EPAQANMDIS TGHMILAYME DHLRNRDRLA KEWQALCAYQ
     AEPNTCAAAQ GEGNVKKNRH PDFLPYDHAR IKLKVESSPS RSDYINASPI IEHDPRMPAY
     IATQGPLSHT IADFWQMVWE SGCTVIVMLT PLVEDGVKQC DRYWPDEGSS LYHVYEVNLV
     SEHIWCEDFL VRSFYLKNVQ TQETRTLTQF HFLSWPAEGT PASTRPLLDF RRKVNKCYRG
     RSCPIIVHCS DGAGRTGTYI LIDMVLNRMA KGVKEIDIAA TLEHVRDQRP GLVRSKDQFE
     FALTAVAEEV NAILKALPQ
//
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