PTPRN_RAT
ID PTPRN_RAT Reviewed; 983 AA.
AC Q63259; Q62883; Q63795; Q64643;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase-like N;
DE Short=R-PTP-N;
DE AltName: Full=105 kDa islet cell antigen;
DE AltName: Full=BEM-3;
DE AltName: Full=Brain-enriched membrane-associated protein tyrosine phosphatase;
DE AltName: Full=ICA105 {ECO:0000303|PubMed:7568143};
DE AltName: Full=ICA512 {ECO:0000303|PubMed:7657822};
DE AltName: Full=PTP IA-2 {ECO:0000303|PubMed:7568143};
DE AltName: Full=PTPLP;
DE Contains:
DE RecName: Full=ICA512-N-terminal fragment;
DE Short=ICA512-NTF;
DE Contains:
DE RecName: Full=ICA512-transmembrane fragment;
DE Short=ICA512-TMF;
DE Contains:
DE RecName: Full=ICA512-cleaved cytosolic fragment;
DE Short=ICA512-CCF;
DE Flags: Precursor;
GN Name=Ptprn;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEOLYTIC CLEAVAGE, AND SUBCELLULAR LOCATION.
RX PubMed=7568143; DOI=10.1073/pnas.92.20.9412;
RA Passini N., Larigan J.D., Genovese S., Appella E., Sinigaglia F., Rogge L.;
RT "The 37/40-kilodalton autoantigen in insulin-dependent diabetes mellitus is
RT the putative tyrosine phosphatase IA-2.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:9412-9416(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=7887886; DOI=10.1042/bj3060331;
RA Kambayashi Y., Takahashi K., Bardhan S., Inagami T.;
RT "Cloning and expression of protein tyrosine phosphatase-like protein
RT derived from a rat pheochromocytoma cell line.";
RL Biochem. J. 306:331-335(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 13-983, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=7657822; DOI=10.1172/jci118188;
RA Payton M.A., Hawkes C.J., Christie M.R.;
RT "Relationship of the 37,000- and 40,000-M(r) tryptic fragments of islet
RT antigens in insulin-dependent diabetes to the protein tyrosine phosphatase-
RT like molecule IA-2 (ICA512).";
RL J. Clin. Invest. 96:1506-1511(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 396-983.
RC STRAIN=Wistar; TISSUE=Brain;
RA Itoh S., Okada M., Nakagawa H.;
RL Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=8641276; DOI=10.1002/j.1460-2075.1996.tb00564.x;
RA Solimena M., Dirkx R. Jr., Hermel J.-M., Pleasic-Williams S., Shapiro J.A.,
RA Caron L., Rabin D.U.;
RT "ICA 512, an autoantigen of type I diabetes, is an intrinsic membrane
RT protein of neurosecretory granules.";
RL EMBO J. 15:2102-2114(1996).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=10457160; DOI=10.1046/j.1460-9568.1999.00677.x;
RA Hermel J.-M., Dirkx R., Solimena M.;
RT "Post-translational modifications of ICA512, a receptor tyrosine
RT phosphatase-like protein of secretory granules.";
RL Eur. J. Neurosci. 11:2609-2620(1999).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=11483505; DOI=10.1093/emboj/20.15.4013;
RA Ort T., Voronov S., Guo J., Zawalich K., Froehner S.C., Zawalich W.,
RA Solimena M.;
RT "Dephosphorylation of beta2-syntrophin and Ca2+/mu-calpain-mediated
RT cleavage of ICA512 upon stimulation of insulin secretion.";
RL EMBO J. 20:4013-4023(2001).
RN [8]
RP PROTEOLYTIC CLEAVAGE.
RX PubMed=15596545; DOI=10.1083/jcb.200408172;
RA Trajkovski M., Mziaut H., Altkrueger A., Ouwendijk J., Knoch K.P.,
RA Mueller S., Solimena M.;
RT "Nuclear translocation of an ICA512 cytosolic fragment couples granule
RT exocytosis and insulin expression in {beta}-cells.";
RL J. Cell Biol. 167:1063-1074(2004).
RN [9]
RP FUNCTION.
RX PubMed=18178618; DOI=10.1073/pnas.0710931105;
RA Mziaut H., Kersting S., Knoch K.P., Fan W.H., Trajkovski M., Erdmann K.,
RA Bergert H., Ehehalt F., Saeger H.D., Solimena M.;
RT "ICA512 signaling enhances pancreatic beta-cell proliferation by regulating
RT cyclins D through STATs.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:674-679(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311 AND SER-312, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Plays a role in vesicle-mediated secretory processes.
CC Required for normal accumulation of secretory vesicles in hippocampus,
CC pituitary and pancreatic islets. Required for the accumulation of
CC normal levels of insulin-containing vesicles and preventing their
CC degradation. Plays a role in insulin secretion in response to glucose
CC stimuli. Required for normal accumulation of the neurotransmitters
CC norepinephrine, dopamine and serotonin in the brain. In females, but
CC not in males, required for normal accumulation and secretion of
CC pituitary hormones, such as luteinizing hormone (LH) and follicle-
CC stimulating hormone (FSH). Required to maintain normal levels of renin
CC expression and renin release. Seems to lack intrinsic enzyme activity.
CC {ECO:0000250|UniProtKB:Q16849, ECO:0000250|UniProtKB:Q60673}.
CC -!- FUNCTION: [ICA512-transmembrane fragment]: ICA512-TMF regulates
CC dynamics and exocytosis of insulin secretory granules (SGs); binding of
CC ICA512-TMF to SNTB2/beta-2-syntrophin is proposed to restrain SGs
CC mobility and exocytosis by tethering them to the actin cytoskeleton
CC depending on UTRN; the function is inhibited by cytoplasmic ICA512-CFF
CC dimerizing with ICA512-TMF and displacing SNTB2 (By similarity).
CC {ECO:0000250|UniProtKB:Q16849}.
CC -!- FUNCTION: [ICA512-cleaved cytosolic fragment]: ICA512-CCF translocated
CC to the nucleus promotes expression of insulin and other granule-related
CC genes; the function implicates binding to and regulating activity of
CC STAT5B probably by preventing its dephosphorylation and potentially by
CC inducing its sumoylation by recruiting PIAS4 (By similarity). Enhances
CC pancreatic beta-cell proliferation by converging with signaling by
CC STAT5B and STAT3 (PubMed:18178618). ICA512-CCF located in the cytoplasm
CC regulates dynamics and exocytosis of insulin secretory granules (SGs)
CC by dimerizing with ICA512-TMF and displacing SNTB2 thus enhancing SGs
CC mobility and exocytosis (By similarity). {ECO:0000250|UniProtKB:Q16849,
CC ECO:0000269|PubMed:18178618}.
CC -!- SUBUNIT: Homodimer; shown for the unprocessed protein (proICA512) in
CC the endoplasmic reticulum and resolved during protein maturation as
CC ICA512-TMF seems to be predominantly monomeric in secretory granules;
CC however, ICA512-CCF interacts with ICA512-TMF disrupting the ICA512-
CC TMF:SNTB2 complex. The isolated lumenal RESP18 homology domain has been
CC shown to form disulfide-linked homooligomers. Interacts (via
CC cytoplasmic domain) with phosphorylated SNTB2; this protects PTPRN
CC against cleavage by CAPN1 to produce ICA512-CCF. Dephosphorylation of
CC SNTB2 upon insulin stimulation disrupts the interaction and results in
CC PTPRN cleavage. Interacts with SNX19. ICA512-CCF interacts with PIAS4;
CC in the nucleus. Interacts with STAT5B (phosphorylated); down-regulated
CC by ICA512-CCF sumoylation; ICA512-CCF prevents STAT5B
CC dephosphorylation; ICA512-CCF mediates interaction of STAT5B with
CC PIAS4. Interacts (via RESP18 homology domain) with insulin and
CC proinsulin. Interacts with PTPRN2, PTPRA and PTPRE.
CC {ECO:0000250|UniProtKB:Q16849, ECO:0000250|UniProtKB:Q60673}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:7568143,
CC ECO:0000305|PubMed:7657822}; Single-pass type I membrane protein
CC {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle membrane
CC {ECO:0000269|PubMed:11483505, ECO:0000269|PubMed:8641276}; Single-pass
CC type I membrane protein {ECO:0000305}. Perikaryon
CC {ECO:0000269|PubMed:8641276}. Cell projection, axon
CC {ECO:0000269|PubMed:8641276}. Synapse {ECO:0000269|PubMed:8641276}.
CC Cell membrane {ECO:0000269|PubMed:8641276}; Single-pass type I membrane
CC protein {ECO:0000305}. Endosome {ECO:0000269|PubMed:8641276}.
CC Note=Detected on neuronal secretory vesicles, but not on synaptic
CC vesicles. Colocalizes with insulin-containing secretory granules.
CC Primarily detected on secretory vesicle membranes. Transiently found at
CC the cell membrane, when secretory vesicles fuse with the cell membrane
CC to release their cargo. Is then endocytosed and recycled to secretory
CC vesicles via the Golgi apparatus membranes.
CC {ECO:0000269|PubMed:8641276}.
CC -!- SUBCELLULAR LOCATION: [ICA512-transmembrane fragment]: Cytoplasmic
CC vesicle, secretory vesicle membrane {ECO:0000269|PubMed:11483505,
CC ECO:0000269|PubMed:8641276}.
CC -!- SUBCELLULAR LOCATION: [ICA512-cleaved cytosolic fragment]: Nucleus
CC {ECO:0000250|UniProtKB:Q16849}.
CC -!- TISSUE SPECIFICITY: Detected in pancreas islets (PubMed:7657822,
CC PubMed:10457160). Detected in pancreas alpha, beta and delta cells, and
CC in chromaffin cells in the adrenal medulla (PubMed:8641276). Detected
CC in amygdala, hypothalamus, autonomous nerve fibers and ganglia,
CC especially at synaptic contacts (PubMed:8641276). Detected in pituitary
CC (at protein level) (PubMed:8641276, PubMed:10457160). Detected in
CC brain, specifically in cerebral cortex, diencephalon and brain stem
CC (PubMed:7887886). {ECO:0000269|PubMed:10457160,
CC ECO:0000269|PubMed:7657822, ECO:0000269|PubMed:7887886,
CC ECO:0000269|PubMed:8641276}.
CC -!- DOMAIN: The RESP18 homology domain is sufficient for targeting
CC proICA512 to secretory granules. {ECO:0000250|UniProtKB:Q16849}.
CC -!- PTM: Subject to proteolytic cleavage at multiple sites
CC (PubMed:7568143). Subject to cleavage on a pair of basic residues (By
CC similarity). Following exocytosis of secretory granules in pancreatic
CC beta-cells ICA512-TMF located in the plasma-membrane is cleaved by mu-
CC type calpain CPN1 to yield ICA512-CCF (PubMed:15596545).
CC {ECO:0000250|UniProtKB:P56722, ECO:0000269|PubMed:15596545,
CC ECO:0000269|PubMed:7568143}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q16849}.
CC -!- PTM: O-glycosylated. {ECO:0000250|UniProtKB:Q16849}.
CC -!- PTM: Sumoylated at two sites including Lys-758. Sumoylation decreases
CC interaction with STAT5. {ECO:0000250|UniProtKB:Q16849}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 8 subfamily. {ECO:0000305}.
CC -!- CAUTION: Does not possess catalytic activity due to replacement of
CC highly conserved residues in tyrosine-protein phosphatase domain.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA07397.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X92563; CAA63313.1; -; mRNA.
DR EMBL; D38222; BAA07397.1; ALT_FRAME; mRNA.
DR EMBL; U40652; AAA83235.1; -; mRNA.
DR EMBL; D45414; BAA08254.1; -; mRNA.
DR PIR; S54342; S54342.
DR RefSeq; NP_446333.1; NM_053881.1.
DR AlphaFoldDB; Q63259; -.
DR SMR; Q63259; -.
DR BioGRID; 250545; 1.
DR IntAct; Q63259; 2.
DR STRING; 10116.ENSRNOP00000026654; -.
DR GlyGen; Q63259; 2 sites.
DR iPTMnet; Q63259; -.
DR PhosphoSitePlus; Q63259; -.
DR jPOST; Q63259; -.
DR PaxDb; Q63259; -.
DR PRIDE; Q63259; -.
DR GeneID; 116660; -.
DR KEGG; rno:116660; -.
DR UCSC; RGD:620777; rat.
DR CTD; 5798; -.
DR RGD; 620777; Ptprn.
DR VEuPathDB; HostDB:ENSRNOG00000019587; -.
DR eggNOG; KOG0793; Eukaryota.
DR HOGENOM; CLU_007905_2_0_1; -.
DR InParanoid; Q63259; -.
DR OMA; AQTGFQI; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; Q63259; -.
DR TreeFam; TF351976; -.
DR PRO; PR:Q63259; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000019587; Expressed in frontal cortex and 15 other tissues.
DR Genevisible; Q63259; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0043679; C:axon terminus; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030141; C:secretory granule; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051020; F:GTPase binding; IPI:RGD.
DR GO; GO:0030507; F:spectrin binding; ISO:RGD.
DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; ISO:RGD.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:RGD.
DR GO; GO:1990502; P:dense core granule maturation; ISO:RGD.
DR GO; GO:0030073; P:insulin secretion; ISO:RGD.
DR GO; GO:0035773; P:insulin secretion involved in cellular response to glucose stimulus; ISS:UniProtKB.
DR GO; GO:0001553; P:luteinization; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:1904692; P:positive regulation of type B pancreatic cell proliferation; IMP:UniProtKB.
DR GO; GO:0051046; P:regulation of secretion; IBA:GO_Central.
DR GO; GO:0051591; P:response to cAMP; IEP:RGD.
DR GO; GO:0043627; P:response to estrogen; IEP:RGD.
DR GO; GO:0009749; P:response to glucose; IEP:RGD.
DR GO; GO:0032868; P:response to insulin; IEP:RGD.
DR GO; GO:0000302; P:response to reactive oxygen species; ISS:UniProtKB.
DR GO; GO:0019932; P:second-messenger-mediated signaling; TAS:RGD.
DR Gene3D; 3.30.70.2470; -; 1.
DR Gene3D; 3.90.190.10; -; 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; PTHR46106; 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 SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Cytoplasmic vesicle; Disulfide bond;
KW Endosome; Glycoprotein; Isopeptide bond; Membrane; Nucleus; Phosphoprotein;
KW Receptor; Reference proteome; Signal; Synapse; Transcription;
KW Transcription regulation; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT SIGNAL 1..40
FT /evidence="ECO:0000250"
FT CHAIN 41..983
FT /note="Receptor-type tyrosine-protein phosphatase-like N"
FT /id="PRO_0000025453"
FT CHAIN 41..452
FT /note="ICA512-N-terminal fragment"
FT /evidence="ECO:0000250|UniProtKB:P56722,
FT ECO:0000250|UniProtKB:Q16849"
FT /id="PRO_0000438085"
FT CHAIN 453..983
FT /note="ICA512-transmembrane fragment"
FT /evidence="ECO:0000250|UniProtKB:P56722,
FT ECO:0000250|UniProtKB:Q16849"
FT /id="PRO_0000438086"
FT CHAIN 663..983
FT /note="ICA512-cleaved cytosolic fragment"
FT /evidence="ECO:0000250|UniProtKB:Q16849"
FT /id="PRO_0000438087"
FT TOPO_DOM 41..579
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 580..604
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 605..983
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 713..973
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 41..137
FT /note="RESP18 homology domain"
FT /evidence="ECO:0000250|UniProtKB:Q16849"
FT REGION 118..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..579
FT /note="Sufficient for dimerization of proICA512"
FT /evidence="ECO:0000250|UniProtKB:Q16849"
FT REGION 605..736
FT /note="Sufficient for dimerization of proICA512"
FT /evidence="ECO:0000250|UniProtKB:P80560"
FT REGION 648..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 452..453
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:P56722"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 46
FT /note="Interchain (with C-46 or C-53); in multimeric form"
FT /evidence="ECO:0000250|UniProtKB:Q16849"
FT DISULFID 53
FT /note="Interchain (with C-46 or C-53); in multimeric form"
FT /evidence="ECO:0000250|UniProtKB:Q16849"
FT DISULFID 59..68
FT /evidence="ECO:0000250|UniProtKB:Q16849"
FT CROSSLNK 758
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:Q16849"
FT CONFLICT 466
FT /note="P -> T (in Ref. 3; AAA83235)"
FT /evidence="ECO:0000305"
FT CONFLICT 507
FT /note="S -> R (in Ref. 3; AAA83235)"
FT /evidence="ECO:0000305"
FT CONFLICT 517
FT /note="A -> V (in Ref. 3; AAA83235)"
FT /evidence="ECO:0000305"
FT CONFLICT 520
FT /note="F -> S (in Ref. 3; AAA83235)"
FT /evidence="ECO:0000305"
FT CONFLICT 564
FT /note="S -> A (in Ref. 3; AAA83235)"
FT /evidence="ECO:0000305"
FT CONFLICT 566
FT /note="A -> E (in Ref. 3; AAA83235)"
FT /evidence="ECO:0000305"
FT CONFLICT 574
FT /note="G -> R (in Ref. 2; BAA07397)"
FT /evidence="ECO:0000305"
FT CONFLICT 581
FT /note="L -> V (in Ref. 3; AAA83235)"
FT /evidence="ECO:0000305"
FT CONFLICT 599
FT /note="A -> V (in Ref. 4; BAA08254)"
FT /evidence="ECO:0000305"
FT CONFLICT 609
FT /note="K -> R (in Ref. 3; AAA83235)"
FT /evidence="ECO:0000305"
FT CONFLICT 664
FT /note="Q -> K (in Ref. 3; AAA83235)"
FT /evidence="ECO:0000305"
FT CONFLICT 672
FT /note="S -> N (in Ref. 3; AAA83235)"
FT /evidence="ECO:0000305"
FT CONFLICT 714
FT /note="A -> P (in Ref. 3; AAA83235)"
FT /evidence="ECO:0000305"
FT CONFLICT 716
FT /note="E -> K (in Ref. 1; CAA63313)"
FT /evidence="ECO:0000305"
FT CONFLICT 731
FT /note="A -> S (in Ref. 3; AAA83235)"
FT /evidence="ECO:0000305"
FT CONFLICT 953..955
FT /note="RPG -> PTC (in Ref. 3; AAA83235)"
FT /evidence="ECO:0000305"
FT CONFLICT 962
FT /note="Q -> K (in Ref. 3; AAA83235)"
FT /evidence="ECO:0000305"
FT CONFLICT 966
FT /note="A -> P (in Ref. 3; AAA83235)"
FT /evidence="ECO:0000305"
FT CONFLICT 969
FT /note="A -> P (in Ref. 3; AAA83235)"
FT /evidence="ECO:0000305"
FT CONFLICT 971
FT /note="A -> G (in Ref. 3; AAA83235)"
FT /evidence="ECO:0000305"
FT CONFLICT 976
FT /note="A -> P (in Ref. 3; AAA83235)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 983 AA; 106228 MW; BCD567DAFFFE2A2B CRC64;
MRRPRRPGGP AGCGGSEGSG GLRLLVCLLL LSGRPGGCSA ISAHGCLFDR RLCSHLEVCI
QDGLFGQCQA GVGQARPLLQ VTSPVLQRLQ GVLRQLMSQG LSWHDDLTQY VISQEMERIP
RLRPPEPHPR DRSGSVPRRA GPAGELLSQG NPTGSSPAVQ GLSRPPGDGN GAGVGSPLSS
LQAELLPPLL EHLLMPPQPP HPSLTYEPAL LQPYLFQQFG SRDGSRGSES ASGVVGHLAK
AEDPVLFSRS LSKAILGTHS GHSFGDLTGP SPAQLFQDSG LLYMAQELPV PGRARAPRLP
EEGGSSRAED SSEGHEEEVL GGHGEKSPPQ AVQADVSLQR LAAVLAGYGV ELRQLTPEQL
STLLTLLQLL PKGTGRHLGG AVNGGADVKK TIEEQMQRGD TADARPPTPL LPGHPTASST
SIKVRQVLSP GFPEPPKTSS PLGISAVLLE KKSPLGQSQP TVVGQPSARP SAEEYGYIVT
DQKPLSLVAG VKLLEILAEH VHMTSGSFIN ISVVGPAVTF RIRHNEQNLS LADVTQQAGL
VKSELEAQTG LQILQTGVGQ REESAAVLPR QAHGISPMRS LLLTLVALAG VAGLLVALAV
ALCMRHHSKQ RDKERLAALG PEGAHGDTTF EYQDLCRQHM ATKSLFNRAE GQPEPSRVSS
VSSQFSDAAQ ASPSSHSSTP SWCEEPAQAN MDISTGHMIL AYMEDHLRNR DRLAKEWQAL
CAYQAEPNTC ATAQGEGNIK KNRHPDFLPY DHARIKLKVE SSPSRSDYIN ASPIIEHDPR
MPAYIATQGP LSHTIADFWQ MVWESGCTVI VMLTPLVEDG VKQCDRYWPD EGSSLYHVYE
VNLVSEHIWC EDFLVRSFYL KNVQTQETRT LTQFHFLSWP AEGTPASTRP LLDFRRKVNK
CYRGRSCPII VHCSDGAGRT GTYILIDMVL NRMAKGVKEI DIAATLEHVR DQRPGLVRSK
DQFEFALTAV AEEVNAILKA LPQ
