ID A0A2I2ZUY9_GORGO Unreviewed; 950 AA.
AC A0A2I2ZUY9;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Protein tyrosine phosphatase receptor type N {ECO:0000313|Ensembl:ENSGGOP00000050933.1};
GN Name=PTPRN {ECO:0000313|Ensembl:ENSGGOP00000050933.1};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000050933.1, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000050933.1, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000050933.1, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000050933.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CABD030018704; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030018705; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_018877926.1; XM_019022381.1.
DR AlphaFoldDB; A0A2I2ZUY9; -.
DR Ensembl; ENSGGOT00000054171.1; ENSGGOP00000050933.1; ENSGGOG00000011854.3.
DR GeneID; 101141224; -.
DR CTD; 5798; -.
DR GeneTree; ENSGT00940000154095; -.
DR OrthoDB; 2911650at2759; -.
DR Proteomes; UP000001519; Chromosome 2B.
DR Bgee; ENSGGOG00000011854; Expressed in frontal cortex and 2 other cell types or tissues.
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 Reference proteome {ECO:0000313|Proteomes:UP000001519};
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..950
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014172661"
FT TRANSMEM 548..571
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 680..940
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 859..931
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 112..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 950 AA; 102955 MW; C567A9158FF69895 CRC64;
MRRPRRPGGL GGSGGLRLLL CLLLLSSRPG GCSAVSAHGC LFDRRLCSHL EVCIQDGLFG
QCQVGVGQAR PLLQVTSPVL QRLQGVLRQL MSQGLSWHDD LTQYVISQEM ERIPRLRPPE
PRPRDRSGLA PKRPGPAEEL LLQDIPTGSA PAAQHRLPQP PVGKGGAGAS SSLSPLQAEL
LPPLLEHLLL PPQPPHPSLS YEPALLQPYL FHQFGSRDGS RVSEGSPGMV SVGPLPKAEA
PALFSRTASK GIFGDHPGHS YGDLPGPSPA QLFQDSGLLY LAQELPAPSR ARVPRLPEQG
GSSRAEDSPE GYEKEGLEGR GEKPVSPAVQ PDAALQRLAA VLAGYGVELR QLTPEQLSTL
LTLLQLLPKG AGRNPGGVVN VGADIKKTME GPVEGRDTAE LPARTPPMPG HPTASPTSSE
VQQVPSPVSS EPPKAARPPA TPVLLEKKSP LGQSQPTVAG QLSARPAAEE YGYIVTDQNV
VGPALTFRIR HNEQNLSLAD VTQQAGLVKS ELEAQTGLQI LQTGVGQREE AAAVLPRTAH
STSPMRSVLL TLVALAGVAG LLVALAVALC VRQHARQRDK ERLAALGPEG AHGDTTFEYQ
DLCRQHMATK SLFNRAEGPP EPSRVSSVSS QFSDAAQASP SSHSSTPSWC EEPAQANMDI
STGHMILAYM EDHLRNRDRL AKEWQALCAY QAEPNTCATA QGEGNIKKNR HPDFLPYDHA
RIKLKVESSP SRSDYINASP IIEHDPRMPA YIATQGPLSH TIADFWQMVW ESGCTVIVML
TPLVEDGVKQ CDRYWPDEGA SLYHVYEVNL VSEHIWCEDF LVRSFYLKNV QTQETRTLTQ
FHFLSWPAEG TPASTRPLLD FRRKVNKCYR GRSCPIIVHC SDGAGRTGTY ILIDMVLNRM
AKGVKEIDIA ATLEHVRDQR PGLVRSKDQF EFALTAVAEE VNAILKALPQ
//
