ID ERF3A_HUMAN Reviewed; 499 AA. AC P15170; J3KQG6; Q96GF2; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 27-MAR-2024, entry version 211. DE RecName: Full=Eukaryotic peptide chain release factor GTP-binding subunit ERF3A; DE Short=Eukaryotic peptide chain release factor subunit 3a; DE Short=eRF3a; DE EC=3.6.5.- {ECO:0000269|PubMed:16777602, ECO:0000305|PubMed:15987998}; DE AltName: Full=G1 to S phase transition protein 1 homolog; GN Name=GSPT1; Synonyms=ERF3A; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=2511002; DOI=10.1002/j.1460-2075.1989.tb08558.x; RA Hoshino S., Miyazawa H., Enomoto T., Hanaoka F., Kikuchi Y., Kikuchi A., RA Ui M.; RT "A human homologue of the yeast GST1 gene codes for a GTP-binding protein RT and is expressed in a proliferation-dependent manner in mammalian cells."; RL EMBO J. 8:3807-3814(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10493829; DOI=10.1006/geno.1999.5927; RA Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J., RA Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X., RA Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C., RA Adams M.D.; RT "Genome duplications and other features in 12 Mb of DNA sequence from human RT chromosome 16p and 16q."; RL Genomics 60:295-308(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=15987998; DOI=10.1128/mcb.25.14.5801-5811.2005; RA Chauvin C., Salhi S., Le Goff C., Viranaicken W., Diop D., Jean-Jean O.; RT "Involvement of human release factors eRF3a and eRF3b in translation RT termination and regulation of the termination complex formation."; RL Mol. Cell. Biol. 25:5801-5811(2005). RN [6] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=16777602; DOI=10.1016/j.cell.2006.04.035; RA Alkalaeva E.Z., Pisarev A.V., Frolova L.Y., Kisselev L.L., Pestova T.V.; RT "In vitro reconstitution of eukaryotic translation reveals cooperativity RT between release factors eRF1 and eRF3."; RL Cell 125:1125-1136(2006). RN [7] RP IDENTIFICATION IN THE SURF COMPLEX, AND FUNCTION. RX PubMed=19417104; DOI=10.1101/gad.1767209; RA Yamashita A., Izumi N., Kashima I., Ohnishi T., Saari B., Katsuhata Y., RA Muramatsu R., Morita T., Iwamatsu A., Hachiya T., Kurata R., Hirano H., RA Anderson P., Ohno S.; RT "SMG-8 and SMG-9, two novel subunits of the SMG-1 complex, regulate RT remodeling of the mRNA surveillance complex during nonsense-mediated mRNA RT decay."; RL Genes Dev. 23:1091-1105(2009). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [9] RP INTERACTION WITH JMJD4. RX PubMed=24486019; DOI=10.1016/j.molcel.2013.12.028; RA Feng T., Yamamoto A., Wilkins S.E., Sokolova E., Yates L.A., Muenzel M., RA Singh P., Hopkinson R.J., Fischer R., Cockman M.E., Shelley J., RA Trudgian D.C., Schoedel J., McCullagh J.S., Ge W., Kessler B.M., RA Gilbert R.J., Frolova L.Y., Alkalaeva E., Ratcliffe P.J., Schofield C.J., RA Coleman M.L.; RT "Optimal translational termination requires C4 lysyl hydroxylation of RT eRF1."; RL Mol. Cell 53:645-654(2014). RN [10] RP FUNCTION, AND INTERACTION WITH SHFL. RX PubMed=30682371; DOI=10.1016/j.cell.2018.12.030; RA Wang X., Xuan Y., Han Y., Ding X., Ye K., Yang F., Gao P., Goff S.P., RA Gao G.; RT "Regulation of HIV-1 Gag-Pol Expression by Shiftless, an Inhibitor of RT Programmed -1 Ribosomal Frameshifting."; RL Cell 176:625.E14-635.E14(2019). RN [11] {ECO:0007744|PDB:3E1Y} RP X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS) OF 301-499 IN CCOMPLEX WITH ETF1, RP FUNCTION, AND IDENTIFICATION IN THE ERF1-ERF3-GTP TERNARY COMPLEX. RX PubMed=19417105; DOI=10.1101/gad.1770109; RA Cheng Z., Saito K., Pisarev A.V., Wada M., Pisareva V.P., Pestova T.V., RA Gajda M., Round A., Kong C., Lim M., Nakamura Y., Svergun D.I., Ito K., RA Song H.; RT "Structural insights into eRF3 and stop codon recognition by eRF1."; RL Genes Dev. 23:1106-1118(2009). RN [12] RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 73-87 (ISOFORM 2). RX PubMed=20418951; DOI=10.1371/journal.pone.0010169; RA Kozlov G., Gehring K.; RT "Molecular basis of eRF3 recognition by the MLLE domain of poly(A)-binding RT protein."; RL PLoS ONE 5:E10169-E10169(2010). RN [13] {ECO:0007744|PDB:5LZT} RP STRUCTURE BY ELECTRON MICROSCOPY (3.65 ANGSTROMS) IN COMPLEX WITH ETF1/ERF1 RP AND RIBOSOME, FUNCTION, AND IDENTIFICATION IN THE ERF1-ERF3-GTP TERNARY RP COMPLEX. RX PubMed=27863242; DOI=10.1016/j.cell.2016.10.046; RA Shao S., Murray J., Brown A., Taunton J., Ramakrishnan V., Hegde R.S.; RT "Decoding mammalian ribosome-mRNA states by translational GTPase RT complexes."; RL Cell 167:1229-1240(2016). CC -!- FUNCTION: GTPase component of the eRF1-eRF3-GTP ternary complex, a CC ternary complex that mediates translation termination in response to CC the termination codons UAA, UAG and UGA (PubMed:2511002, CC PubMed:15987998, PubMed:19417105, PubMed:27863242). GSPT1/ERF3A CC mediates ETF1/ERF1 delivery to stop codons: The eRF1-eRF3-GTP complex CC binds to a stop codon in the ribosomal A-site (PubMed:27863242). GTP CC hydrolysis by GSPT1/ERF3A induces a conformational change that leads to CC its dissociation, permitting ETF1/ERF1 to accommodate fully in the A- CC site (PubMed:16777602, PubMed:27863242). Component of the transient CC SURF complex which recruits UPF1 to stalled ribosomes in the context of CC nonsense-mediated decay (NMD) of mRNAs containing premature stop codons CC (PubMed:24486019). Required for SHFL-mediated translation termination CC which inhibits programmed ribosomal frameshifting (-1PRF) of mRNA from CC viruses and cellular genes (PubMed:30682371). CC {ECO:0000269|PubMed:15987998, ECO:0000269|PubMed:16777602, CC ECO:0000269|PubMed:19417105, ECO:0000269|PubMed:24486019, CC ECO:0000269|PubMed:2511002, ECO:0000269|PubMed:27863242, CC ECO:0000269|PubMed:30682371}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; CC Evidence={ECO:0000269|PubMed:16777602, ECO:0000305|PubMed:15987998}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; CC Evidence={ECO:0000305|PubMed:15987998}; CC -!- SUBUNIT: Component of the eRF1-eRF3-GTP ternary complex, composed of CC ETF1/ERF1 and ERF3 (GSPT1/ERF3A or GSPT2/ERF3B) and GTP CC (PubMed:19417105, PubMed:27863242). Component of the transient SURF CC (SMG1-UPF1-eRF1-eRF3) complex (PubMed:19417104). The ETF1-GSPT1 complex CC interacts with JMJD4 (PubMed:24486019). Interacts with PABPC1 (By CC similarity). Interacts with SHFL (PubMed:30682371). CC {ECO:0000250|UniProtKB:Q8R050, ECO:0000269|PubMed:19417104, CC ECO:0000269|PubMed:19417105, ECO:0000269|PubMed:24486019, CC ECO:0000269|PubMed:27863242, ECO:0000269|PubMed:30682371}. CC -!- INTERACTION: CC P15170; P62495: ETF1; NbExp=4; IntAct=EBI-948993, EBI-750990; CC P15170; Q92900: UPF1; NbExp=2; IntAct=EBI-948993, EBI-373471; CC P15170-2; P11940: PABPC1; NbExp=2; IntAct=EBI-9094806, EBI-81531; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P15170-1; Sequence=Displayed; CC Name=2; CC IsoId=P15170-2; Sequence=VSP_042198, VSP_042199; CC Name=3; CC IsoId=P15170-3; Sequence=VSP_042198; CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. ERF3 subfamily. CC {ECO:0000255|PROSITE-ProRule:PRU01059}. CC -!- CAUTION: eRF3 antibodies used in PubMed:19417104 do not differentiate CC between GSPT1/ERF3A and GSPT2/ERF3B. {ECO:0000305}. 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; X17644; CAA35635.1; -; mRNA. DR EMBL; U95742; AAB67250.1; -; Genomic_DNA. DR EMBL; AC007216; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC009503; AAH09503.2; -; mRNA. DR CCDS; CCDS45412.1; -. [P15170-3] DR CCDS; CCDS45413.1; -. [P15170-2] DR CCDS; CCDS45414.1; -. [P15170-1] DR PIR; S06941; S06941. DR RefSeq; NP_001123478.1; NM_001130006.1. [P15170-2] DR RefSeq; NP_001123479.1; NM_001130007.1. [P15170-1] DR PDB; 3E1Y; X-ray; 3.80 A; E/F/G/H=301-499. DR PDB; 3J5Y; EM; 9.70 A; B=69-496. DR PDB; 3KUI; X-ray; 2.30 A; B=64-78. DR PDB; 4D61; EM; 9.00 A; i=72-497. DR PDB; 5HXB; X-ray; 3.60 A; A/X=300-496. DR PDB; 5LZT; EM; 3.65 A; jj=1-499. DR PDB; 6XK9; X-ray; 3.64 A; A/X=300-496. DR PDBsum; 3E1Y; -. DR PDBsum; 3J5Y; -. DR PDBsum; 3KUI; -. DR PDBsum; 4D61; -. DR PDBsum; 5HXB; -. DR PDBsum; 5LZT; -. DR PDBsum; 6XK9; -. DR AlphaFoldDB; P15170; -. DR EMDB; EMD-4131; -. DR EMDB; EMD-5801; -. DR SMR; P15170; -. DR BioGRID; 109190; 298. DR ComplexPortal; CPX-2721; Translation release factor ERF1-ERF3 complex. DR CORUM; P15170; -. DR IntAct; P15170; 27. DR MINT; P15170; -. DR STRING; 9606.ENSP00000398131; -. DR BindingDB; P15170; -. DR ChEMBL; CHEMBL4523593; -. DR DrugBank; DB04315; Guanosine-5'-Diphosphate. DR GlyGen; P15170; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P15170; -. DR MetOSite; P15170; -. DR PhosphoSitePlus; P15170; -. DR SwissPalm; P15170; -. DR BioMuta; GSPT1; -. DR DMDM; 121688; -. DR EPD; P15170; -. DR jPOST; P15170; -. DR MassIVE; P15170; -. DR MaxQB; P15170; -. DR PaxDb; 9606-ENSP00000398131; -. DR PeptideAtlas; P15170; -. DR ProteomicsDB; 53116; -. [P15170-1] DR ProteomicsDB; 53117; -. [P15170-2] DR Pumba; P15170; -. DR Antibodypedia; 24757; 200 antibodies from 30 providers. DR DNASU; 2935; -. DR Ensembl; ENST00000420576.6; ENSP00000399539.2; ENSG00000103342.13. [P15170-1] DR Ensembl; ENST00000434724.7; ENSP00000398131.2; ENSG00000103342.13. [P15170-3] DR Ensembl; ENST00000439887.6; ENSP00000408399.2; ENSG00000103342.13. [P15170-2] DR Ensembl; ENST00000563468.5; ENSP00000454351.1; ENSG00000103342.13. [P15170-1] DR GeneID; 2935; -. DR KEGG; hsa:2935; -. DR MANE-Select; ENST00000434724.7; ENSP00000398131.2; NM_002094.4; NP_002085.3. [P15170-3] DR UCSC; uc002dbt.4; human. [P15170-1] DR AGR; HGNC:4621; -. DR CTD; 2935; -. DR DisGeNET; 2935; -. DR GeneCards; GSPT1; -. DR HGNC; HGNC:4621; GSPT1. DR HPA; ENSG00000103342; Low tissue specificity. DR MIM; 139259; gene. DR neXtProt; NX_P15170; -. DR OpenTargets; ENSG00000103342; -. DR PharmGKB; PA29012; -. DR VEuPathDB; HostDB:ENSG00000103342; -. DR eggNOG; KOG0459; Eukaryota. DR GeneTree; ENSGT00940000155582; -. DR HOGENOM; CLU_007265_3_8_1; -. DR InParanoid; P15170; -. DR OMA; GKMESGC; -. DR OrthoDB; 5477300at2759; -. DR PhylomeDB; P15170; -. DR TreeFam; TF300566; -. DR PathwayCommons; P15170; -. DR Reactome; R-HSA-72764; Eukaryotic Translation Termination. DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs. DR Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC). DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC). DR SignaLink; P15170; -. DR SIGNOR; P15170; -. DR BioGRID-ORCS; 2935; 786 hits in 1166 CRISPR screens. DR ChiTaRS; GSPT1; human. DR EvolutionaryTrace; P15170; -. DR GeneWiki; GSPT1; -. DR GenomeRNAi; 2935; -. DR Pharos; P15170; Tbio. DR PRO; PR:P15170; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; P15170; Protein. DR Bgee; ENSG00000103342; Expressed in gingival epithelium and 209 other cell types or tissues. DR ExpressionAtlas; P15170; baseline and differential. DR GO; GO:0005737; C:cytoplasm; NAS:ComplexPortal. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0022626; C:cytosolic ribosome; IDA:UniProt. DR GO; GO:0018444; C:translation release factor complex; IDA:UniProtKB. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0003747; F:translation release factor activity; IDA:UniProtKB. DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:UniProtKB. DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:UniProtKB. DR GO; GO:0006479; P:protein methylation; IDA:MGI. DR GO; GO:0006449; P:regulation of translational termination; IMP:UniProtKB. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR GO; GO:0006415; P:translational termination; IDA:UniProtKB. DR CDD; cd01883; EF1_alpha; 1. DR CDD; cd03704; eRF3_C_III; 1. DR CDD; cd04089; eRF3_II; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 2.40.30.10; Translation factors; 2. DR InterPro; IPR004161; EFTu-like_2. DR InterPro; IPR031157; G_TR_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000795; T_Tr_GTP-bd_dom. DR InterPro; IPR009000; Transl_B-barrel_sf. DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C. DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C. DR PANTHER; PTHR23115:SF125; EUKARYOTIC PEPTIDE CHAIN RELEASE FACTOR GTP-BINDING SUBUNIT ERF3A; 1. DR PANTHER; PTHR23115; TRANSLATION FACTOR; 1. DR Pfam; PF00009; GTP_EFTU; 1. DR Pfam; PF03144; GTP_EFTU_D2; 1. DR Pfam; PF03143; GTP_EFTU_D3; 1. DR PRINTS; PR00315; ELONGATNFCT. DR SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF50447; Translation proteins; 1. DR PROSITE; PS00301; G_TR_1; 1. DR PROSITE; PS51722; G_TR_2; 1. DR Genevisible; P15170; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; GTP-binding; Hydrolase; KW Nonsense-mediated mRNA decay; Nucleotide-binding; Protein biosynthesis; KW Reference proteome. FT CHAIN 1..499 FT /note="Eukaryotic peptide chain release factor GTP-binding FT subunit ERF3A" FT /id="PRO_0000091480" FT DOMAIN 72..298 FT /note="tr-type G" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 1..69 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 81..88 FT /note="G1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 137..141 FT /note="G2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 158..161 FT /note="G3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 220..223 FT /note="G4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 262..264 FT /note="G5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT COMPBIAS 16..30 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 42..60 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 84..89 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:O74718" FT BINDING 220..223 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:O74718" FT BINDING 262..264 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:O74718" FT VAR_SEQ 1 FT /note="M -> MDPGSGGGGGGGGGGGSSSGSSSSDSAPDCWDQADMEAPGPGPCGGG FT GSLAAAAEAQRENLSAAFSRQLNVNAKPFVPNVHAAEFVPSFLRGPAAPPPPVGGAANN FT HGAGSGAGGRAAPVESSQEEQSLCEGSNSAVSM (in isoform 2 and isoform FT 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_042198" FT VAR_SEQ 8 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_042199" FT CONFLICT P15170-2:6..9 FT /note="GGGG -> G (in Ref. 4; AAH09503)" FT /evidence="ECO:0000305" FT CONFLICT P15170-2:92 FT /note="G -> C (in Ref. 4; AAH09503)" FT /evidence="ECO:0000305" FT CONFLICT P15170-2:100 FT /note="V -> A (in Ref. 4; AAH09503)" FT /evidence="ECO:0000305" SQ SEQUENCE 499 AA; 55756 MW; DE20482CCABC3576 CRC64; MELSEPIVEN GETEMSPEES WEHKEEISEA EPGGGSLGDG RPPEESAHEM MEEEEEIPKP KSVVAPPGAP KKEHVNVVFI GHVDAGKSTI GGQIMYLTGM VDKRTLEKYE REAKEKNRET WYLSWALDTN QEERDKGKTV EVGRAYFETE KKHFTILDAP GHKSFVPNMI GGASQADLAV LVISARKGEF ETGFEKGGQT REHAMLAKTA GVKHLIVLIN KMDDPTVNWS NERYEECKEK LVPFLKKVGF NPKKDIHFMP CSGLTGANLK EQSDFCPWYI GLPFIPYLDN LPNFNRSVDG PIRLPIVDKY KDMGTVVLGK LESGSICKGQ QLVMMPNKHN VEVLGILSDD VETDTVAPGE NLKIRLKGIE EEEILPGFIL CDPNNLCHSG RTFDAQIVII EHKSIICPGY NAVLHIHTCI EEVEITALIC LVDKKSGEKS KTRPRFVKQD QVCIARLRTA GTICLETFKD FPQMGRFTLR DEGKTIAIGK VLKLVPEKD //