ID F120A_HUMAN Reviewed; 1118 AA. AC Q9NZB2; A6NGU0; C4AMC6; O60649; Q14688; Q4VXF4; Q4VXF5; Q4VXG2; Q86V69; AC Q96I21; Q9NZB1; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 2. DT 27-MAR-2024, entry version 183. DE RecName: Full=Constitutive coactivator of PPAR-gamma-like protein 1; DE AltName: Full=Oxidative stress-associated SRC activator {ECO:0000303|PubMed:19015244}; DE AltName: Full=Protein FAM120A; GN Name=FAM120A; GN Synonyms=C9orf10, KIAA0183, OSSA {ECO:0000303|PubMed:19015244}; 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 B), AND NUCLEOTIDE SEQUENCE [MRNA] OF RP 1-1102 (ISOFORM A). RA Brahmbhatt S.B., Hulme D.J., Dawkins J.L., Nicholson G.A.; RT "Generating full-length coding sequence for 2 alternate transcripts of a RT novel gene C9orf10 and screening HSN-I patients for mutations."; RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 157-1118 (ISOFORM E). RC TISSUE=Lung, and Placenta; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-1069 (ISOFORM A). RC TISSUE=Bone marrow; RX PubMed=8724849; DOI=10.1093/dnares/3.1.17; RA Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.; RT "Prediction of the coding sequences of unidentified human genes. V. The RT coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of RT cDNA clones from human cell line KG-1."; RL DNA Res. 3:17-24(1996). RN [5] RP SEQUENCE REVISION. RA Ohara O., Nagase T., Kikuno R., Nomura N.; RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 393-512 (ISOFORM F), AND TISSUE SPECIFICITY. RX PubMed=14585507; DOI=10.1016/s0378-1119(03)00770-4; RA Holden S., Raymond F.L.; RT "The human gene CXorf17 encodes a member of a novel family of putative RT transmembrane proteins: cDNA cloning and characterization of CXorf17 and RT its mouse ortholog orf34."; RL Gene 318:149-161(2003). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 579-1069 (ISOFORM D). RC TISSUE=Brain; RA Yu W., Gibbs R.A.; RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases. RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1023, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [10] RP FUNCTION, INTERACTION WITH IGF2BP1; FYN; PIK3R1; SRC AND YES1, SUBCELLULAR RP LOCATION, PHOSPHORYLATION, TISSUE SPECIFICITY, AND POTENTIAL ROLE IN CANCER RP PROGRESSION. RX PubMed=19015244; DOI=10.1128/mcb.01035-08; RA Tanaka M., Sasaki K., Kamata R., Hoshino Y., Yanagihara K., Sakai R.; RT "A novel RNA-binding protein, Ossa/C9orf10, regulates activity of Src RT kinases to protect cells from oxidative stress-induced apoptosis."; RL Mol. Cell. Biol. 29:402-413(2009). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1044; SER-1045 AND SER-1048, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [12] 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-655 AND SER-1023, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-960, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [15] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-873; ARG-884; ARG-886; ARG-982 RP AND ARG-986, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). CC -!- FUNCTION: Component of the oxidative stress-induced survival signaling. CC May regulate the activation of SRC family protein kinases CC (PubMed:19015244). May act as a scaffolding protein enabling SRC family CC protein kinases to phosphorylate and activate PI3-kinase CC (PubMed:19015244). Binds IGF2 RNA and promotes the production of IGF2 CC protein (PubMed:19015244). {ECO:0000269|PubMed:19015244}. CC -!- SUBUNIT: Interacts with PURA (By similarity). Interacts with SRC family CC protein kinases YES1, SRC and FYN (PubMed:19015244). Upon tyrosine CC phosphorylation, interacts with PIK3R1 (PubMed:19015244). Interacts CC with IGF2BP1/IMP-1 in an RNA-dependent manner (PubMed:19015244). CC {ECO:0000250|UniProtKB:Q6A0A9, ECO:0000269|PubMed:19015244}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19015244}. Cell CC membrane {ECO:0000269|PubMed:19015244}; Peripheral membrane protein CC {ECO:0000305|PubMed:19015244}; Cytoplasmic side CC {ECO:0000305|PubMed:19015244}. Note=Translocates from the cytosol to CC plasma membrane after UV irradiation. {ECO:0000269|PubMed:19015244}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=A; CC IsoId=Q9NZB2-1; Sequence=Displayed; CC Name=B; CC IsoId=Q9NZB2-2; Sequence=VSP_004147, VSP_004148; CC Name=D; CC IsoId=Q9NZB2-4; Sequence=VSP_017280; CC Name=E; CC IsoId=Q9NZB2-5; Sequence=VSP_017278, VSP_017279; CC Name=F; CC IsoId=Q9NZB2-6; Sequence=VSP_036324; CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:14585507). In gastric CC mucosa, detected in the bottom region of the foveolar epithelium (at CC protein level) (PubMed:19015244). {ECO:0000269|PubMed:14585507, CC ECO:0000269|PubMed:19015244}. CC -!- PTM: Arg-982 is dimethylated, probably to asymmetric dimethylarginine. CC {ECO:0000269|PubMed:24129315}. CC -!- PTM: Phosphorylated on tyrosine by SRC family protein kinases upon CC oxidative stress, for instance following UV irradiation. CC {ECO:0000269|PubMed:19015244}. CC -!- DISEASE: Note=May play a role in the progression of scirrhous-type CC gastric cancer by supporting cancer cell survival during oxidative CC stress. {ECO:0000269|PubMed:19015244}. CC -!- SIMILARITY: Belongs to the constitutive coactivator of PPAR-gamma CC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF72866.1; Type=Frameshift; Evidence={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; AF214737; AAF72866.1; ALT_FRAME; mRNA. DR EMBL; AF214738; AAF72867.1; -; mRNA. DR EMBL; AL353629; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC007879; AAH07879.2; -; mRNA. DR EMBL; BC098584; AAH98584.1; -; mRNA. DR EMBL; BC111736; AAI11737.1; -; mRNA. DR EMBL; D80005; BAA11500.2; -; mRNA. DR EMBL; AY266457; AAP31031.1; -; mRNA. DR EMBL; AF055017; AAC09364.1; -; mRNA. DR CCDS; CCDS6706.1; -. [Q9NZB2-1] DR CCDS; CCDS75859.1; -. [Q9NZB2-2] DR RefSeq; NP_001273651.1; NM_001286722.1. DR RefSeq; NP_001273652.1; NM_001286723.1. [Q9NZB2-5] DR RefSeq; NP_001273653.1; NM_001286724.1. [Q9NZB2-2] DR RefSeq; NP_055427.2; NM_014612.4. [Q9NZB2-1] DR RefSeq; XP_011516714.1; XM_011518412.2. [Q9NZB2-6] DR AlphaFoldDB; Q9NZB2; -. DR BioGRID; 116805; 355. DR IntAct; Q9NZB2; 88. DR MINT; Q9NZB2; -. DR STRING; 9606.ENSP00000277165; -. DR ChEMBL; CHEMBL4295966; -. DR GlyGen; Q9NZB2; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9NZB2; -. DR PhosphoSitePlus; Q9NZB2; -. DR SwissPalm; Q9NZB2; -. DR BioMuta; FAM120A; -. DR DMDM; 158523294; -. DR EPD; Q9NZB2; -. DR jPOST; Q9NZB2; -. DR MassIVE; Q9NZB2; -. DR MaxQB; Q9NZB2; -. DR PaxDb; 9606-ENSP00000277165; -. DR PeptideAtlas; Q9NZB2; -. DR ProteomicsDB; 83345; -. [Q9NZB2-1] DR ProteomicsDB; 83346; -. [Q9NZB2-2] DR ProteomicsDB; 83347; -. [Q9NZB2-4] DR ProteomicsDB; 83348; -. [Q9NZB2-5] DR ProteomicsDB; 83349; -. [Q9NZB2-6] DR Pumba; Q9NZB2; -. DR Antibodypedia; 13858; 158 antibodies from 30 providers. DR DNASU; 23196; -. DR Ensembl; ENST00000277165.11; ENSP00000277165.5; ENSG00000048828.18. [Q9NZB2-1] DR Ensembl; ENST00000375389.7; ENSP00000364538.3; ENSG00000048828.18. [Q9NZB2-2] DR GeneID; 23196; -. DR KEGG; hsa:23196; -. DR MANE-Select; ENST00000277165.11; ENSP00000277165.5; NM_014612.5; NP_055427.2. DR UCSC; uc004atv.5; human. [Q9NZB2-1] DR AGR; HGNC:13247; -. DR CTD; 23196; -. DR DisGeNET; 23196; -. DR GeneCards; FAM120A; -. DR HGNC; HGNC:13247; FAM120A. DR HPA; ENSG00000048828; Low tissue specificity. DR MIM; 612265; gene. DR neXtProt; NX_Q9NZB2; -. DR OpenTargets; ENSG00000048828; -. DR PharmGKB; PA134954136; -. DR VEuPathDB; HostDB:ENSG00000048828; -. DR eggNOG; ENOG502QQNQ; Eukaryota. DR GeneTree; ENSGT00530000063168; -. DR HOGENOM; CLU_008339_2_0_1; -. DR InParanoid; Q9NZB2; -. DR OMA; YILSPQY; -. DR OrthoDB; 20093at2759; -. DR PhylomeDB; Q9NZB2; -. DR TreeFam; TF328642; -. DR PathwayCommons; Q9NZB2; -. DR SignaLink; Q9NZB2; -. DR BioGRID-ORCS; 23196; 27 hits in 1153 CRISPR screens. DR ChiTaRS; FAM120A; human. DR GeneWiki; FAM120A; -. DR GenomeRNAi; 23196; -. DR Pharos; Q9NZB2; Tbio. DR PRO; PR:Q9NZB2; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q9NZB2; Protein. DR Bgee; ENSG00000048828; Expressed in tibia and 217 other cell types or tissues. DR ExpressionAtlas; Q9NZB2; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR Gene3D; 3.40.50.1010; 5'-nuclease; 1. DR InterPro; IPR026784; Coact_PPARg. DR InterPro; IPR029060; PIN-like_dom_sf. DR PANTHER; PTHR15976; CONSTITUTIVE COACTIVATOR OF PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR GAMMA; 1. DR PANTHER; PTHR15976:SF14; CONSTITUTIVE COACTIVATOR OF PPAR-GAMMA-LIKE PROTEIN 1; 1. DR SUPFAM; SSF88723; PIN domain-like; 1. DR Genevisible; Q9NZB2; HS. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Cell membrane; Cytoplasm; Membrane; KW Methylation; Phosphoprotein; Reference proteome; RNA-binding; KW Tumor suppressor. FT CHAIN 1..1118 FT /note="Constitutive coactivator of PPAR-gamma-like protein FT 1" FT /id="PRO_0000221627" FT REGION 339..405 FT /note="Interaction with YES1, SRC and FYN" FT /evidence="ECO:0000269|PubMed:19015244" FT REGION 374..533 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 829..1118 FT /note="RNA binding" FT /evidence="ECO:0000269|PubMed:19015244" FT REGION 921..945 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1025..1102 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 401..423 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 434..485 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 501..521 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 921..940 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1068..1098 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 655 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 873 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 884 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 886 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 932 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q6A0A9" FT MOD_RES 960 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 982 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 986 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 1023 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18220336, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1044 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 1045 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 1048 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT VAR_SEQ 473 FT /note="N -> KPFQLYLQKNFVFHKENSIVLCSRILRHG (in isoform F)" FT /evidence="ECO:0000303|PubMed:14585507" FT /id="VSP_036324" FT VAR_SEQ 579..628 FT /note="GEIKIAVSIEDEANKDLPPAALLYRPVRQYVYGVLFSLAESRKKTERLAF FT -> VLSKGPWSGFCYLMSGHSYGCFVLLSFFEPFFCLTNLLETKFTFPFLNIE (in FT isoform B)" FT /evidence="ECO:0000303|Ref.1" FT /id="VSP_004147" FT VAR_SEQ 629..1118 FT /note="Missing (in isoform B)" FT /evidence="ECO:0000303|Ref.1" FT /id="VSP_004148" FT VAR_SEQ 637..651 FT /note="FSPVIIKEWAAYKGK -> CMYCNNPLFVFLGTS (in isoform E)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_017278" FT VAR_SEQ 652..1118 FT /note="Missing (in isoform E)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_017279" FT VAR_SEQ 890..935 FT /note="Missing (in isoform D)" FT /evidence="ECO:0000303|Ref.7" FT /id="VSP_017280" FT VARIANT 327 FT /note="Y -> H (in dbSNP:rs11541747)" FT /id="VAR_054400" FT CONFLICT 517..520 FT /note="EGKG -> DSRR (in Ref. 1; AAF72867)" FT /evidence="ECO:0000305" FT CONFLICT 556 FT /note="L -> V (in Ref. 1; AAF72867)" FT /evidence="ECO:0000305" SQ SEQUENCE 1118 AA; 121888 MW; C9171EA01C8D17A0 CRC64; MGVQGFQDYI EKHCPSAVVP VELQKLARGS LVGGGRQRPP QTPLRLLVDA DNCLHRLYGG FYTDWVSGGQ WNHMLGYLAA LAKACFGGNI ELFVFFNGAL EKARLHEWVK RQGNERQTAQ QIVSHVQNKG TPPPKVWFLP PVCMAHCIRL ALIRFHVKVA QSIEDHHQEV IGFCRENGFH GLVAYDSDYA LCNIPYYFSA HALKLSRNGK SLTTSQYLMH EVAKQLDLNP NRFPIFAALL GNHILPDEDL ASFHWSLLGP EHPLASLKVR AHQLVLPPCD VVIKAVADYV RNIQDTSDLD AIAKDVFQHS QSRTDDKVIR FKRAIGYYSA TSKPMSFHPP HYLAARPGPF GMPGMVPPHV PPQMLNIPQT SLQAKPVAPQ VPSPGGAPGQ GPYPYSLSEP APLTLDTSGK NLTEQNSYSN IPHEGKHTPL YERSSPINPA QSGSPNHVDS AYFPGSSTSS SSDNDEGSGG ATNHISGNKI GWEKTGSHSE PQARGDPGDQ TKAEGSSTAS SGSQLAEGKG SQMGTVQPIP CLLSMPTRNH MDITTPPLPP VAPEVLRVAE HRHKKGLMYP YIFHVLTKGE IKIAVSIEDE ANKDLPPAAL LYRPVRQYVY GVLFSLAESR KKTERLAFRK NRLPPEFSPV IIKEWAAYKG KSPQTPELVE ALAFREWTCP NLKRLWLGKA VEDKNRRMRA FLACMRSDTP AMLNPANVPT HLMVLCCVLR YMVQWPGARI LRRQELDAFL AQALSPKLYE PDQLQELKIE NLDPRGIQLS ALFMSGVDMA LFANDACGQP IPWEHCCPWM YFDGKLFQSK LLKASREKTP LIDLCDGQAD QAAKVEKMRQ SVLEGLSFSR QSHTLPFPPP PALPFYPASA YPRHFGPVPP SQGRGRGFAG VCGFGGPYGE TVATGPYRAF RVAAASGHCG AFSGSDSSRT SKSQGGVQPI PSQGGKLEIA GTVVGHWAGS RRGRGGRGPF PLQVVSVGGP ARGRPRGVIS TPVIRTFGRG GRYYGRGYKN QAAIQGRPPY AASAEEVAKE LKSKSGESKS SAMSSDGSLA ENGVMAEEKP APQMNGSTGD ARAPSHSESA LNNDSKTCNT NPHLNALSTD SACRREAALE AAVLNKEE //