ID H2RKV0_TAKRU Unreviewed; 920 AA.
AC H2RKV0;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Receptor-type tyrosine-protein phosphatase-like N {ECO:0000313|Ensembl:ENSTRUP00000000763.3};
GN Name=PTPRN {ECO:0000313|Ensembl:ENSTRUP00000000763.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000000763.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000000763.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000000763.3}
RP IDENTIFICATION.
RG Ensembl;
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 AlphaFoldDB; H2RKV0; -.
DR STRING; 31033.ENSTRUP00000082549; -.
DR Ensembl; ENSTRUT00000000766.3; ENSTRUP00000000763.3; ENSTRUG00000000335.3.
DR GeneTree; ENSGT00940000154095; -.
DR HOGENOM; CLU_001645_9_9_1; -.
DR Proteomes; UP000005226; Chromosome 8.
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 Reference proteome {ECO:0000313|Proteomes:UP000005226};
KW Signal {ECO:0000256|SAM:SignalP}; Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..920
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025527787"
FT DOMAIN 650..910
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 829..901
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 118..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 920 AA; 101538 MW; 3F29110917B02E19 CRC64;
MLSPRLWAAL GRLLLLFTAS CPLCETARHG CLFEKNLCRS DQLCSNDGLF GECQAAHQQP
VQYQVSVQTL HKLQEVLKDL MVQGLTWRDD LTQDIIGREL SHIPTVSSSF KPHEKMTNRL
EDSQHSHSSR PTQTCAGTNP NSHFRQLEPS QQRVRLVENI ADPDVMQQYV DYMILDPSQS
SVRMQTPLLD PYTYRQQFGF QDEEERSINS LDDLHAPSSR SRSGGNSRDR DKQLLQDLVS
FYLSAPSSSS SSSSPVQTLS RNRGRTGFPS SSSSSSFFHN LDFPLDYGED YVSQMTQLRQ
QQQQQQQQQA EKNKMQEEYG TLSGLDDRSL RRLALLLDHL DLDAKDSSPE QENKPLATPK
QLQLEGPYGY KQSKGLTASK HQTYGNKAAT GEKVKSKSHL LRRQLKLVRG SDGVSAVCFA
GSVVGPAVTF RIRPNSKNLT SADVAEKAVA EKNILESKTG LKVLQSGVGE GGNGKALPLA
TRVQPPSRWA FTTLVLMACL GSVLVAGMTI ACLRHYAHRL AAKKLGLGPE AGSFSHQEYQ
DLCRQHMASK GAFGRLEAAA LGAVGGASGR GGGGAGVSGA AGGGASVGGG VDSRVSSVSS
QFSDGAQPSP SSHSSTPSWC EEPAQANMDI STGHMILAYM EDHLRNKNRL MKEWEALCSY
QAEPSAVSVA QSDANAKKNR CPDSVPYDHS RVKLKAEINP SRSDYINAST IIEHDPRMPA
YIATQGPLSH TISDFWQMVW ENGCTVIVMM TALVEDGEKQ CDRYWPDEGS SLYHIYEVNL
VSEHIWCNDF LVRSFYLKNV QTQETRTLTQ FHFLSWPAQG IPTSTRPLLD FRRKVNKCYR
GRSCPIIVHC SDGTGRTGTY ILIDMVLNRM AKGVKEIDIA ATLEHVRDQR PGMVRTKDQF
EFALTAVAEE VNAILKALPQ
//
