F120A_HUMAN
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 03-AUG-2022, entry version 174.
DE RecName: Full=Constitutive coactivator of PPAR-gamma-like protein 1;
DE AltName: Full=Oxidative stress-associated Src activator;
DE AltName: Full=Protein FAM120A;
GN Name=FAM120A; Synonyms=C9orf10, KIAA0183, OSSA;
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 YES1; SRC AND FYN, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
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: May participate in mRNA transport in the cytoplasm (By
CC similarity). Critical component of the oxidative stress-induced
CC survival signaling. Activates src family kinases and acts as a
CC scaffolding protein enabling src family kinases to phosphorylate and
CC activate PI3-kinase. Binds RNA and promotes the secretion of IGF-II.
CC May play a pivotal role in the progression of scirrhous-type gastric
CC cancer by supporting cancer cell survival in environments with various
CC oxidative stresses. {ECO:0000250, ECO:0000269|PubMed:19015244}.
CC -!- SUBUNIT: Interacts with PURA (By similarity). Interacts with YES1, SRC,
CC FYN. Upon tyrosine phosphorylation, interacts with PIK3R1.
CC {ECO:0000250, ECO:0000269|PubMed:19015244}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19015244}. Cell
CC membrane {ECO:0000269|PubMed:19015244}; Peripheral membrane protein
CC {ECO:0000269|PubMed:19015244}; Cytoplasmic side
CC {ECO:0000269|PubMed:19015244}. Note=Translocates to plasma membrane
CC upon ultraviolet exposure.
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: Ubiquitously expressed. Highly expressed in
CC scirrhous-type gastric cancer tissues compared with normal gastric
CC mucosa (at protein level). {ECO:0000269|PubMed:14585507,
CC ECO:0000269|PubMed:19015244}.
CC -!- PTM: Arg-982 is dimethylated, probably to asymmetric dimethylarginine.
CC -!- PTM: Phosphorylated on tyrosine by src family kinases upon ultraviolet
CC exposure.
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};
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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; 307.
DR IntAct; Q9NZB2; 77.
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; Q9NZB2; -.
DR PeptideAtlas; Q9NZB2; -.
DR PRIDE; 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 Antibodypedia; 13858; 135 antibodies from 30 providers.
DR DNASU; 23196; -.
DR Ensembl; ENST00000277165.11; ENSP00000277165.5; ENSG00000048828.17. [Q9NZB2-1]
DR Ensembl; ENST00000375389.7; ENSP00000364538.3; ENSG00000048828.17. [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 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; NDGLMRG; -.
DR OrthoDB; 203269at2759; -.
DR PhylomeDB; Q9NZB2; -.
DR TreeFam; TF328642; -.
DR PathwayCommons; Q9NZB2; -.
DR SignaLink; Q9NZB2; -.
DR BioGRID-ORCS; 23196; 19 hits in 1077 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 215 other tissues.
DR ExpressionAtlas; Q9NZB2; baseline and differential.
DR Genevisible; Q9NZB2; HS.
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 InterPro; IPR026784; Coact_PPARg.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR PANTHER; PTHR15976; PTHR15976; 1.
DR SUPFAM; SSF88723; SSF88723; 1.
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 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
