FAKD4_HUMAN
ID FAKD4_HUMAN Reviewed; 631 AA.
AC Q969Z0; A4D2L2; A4D2L3; D3DVL5; D3DVL6; O14710; Q53GI8; Q8NDM4; Q9BUC6;
AC Q9Y2F6;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=FAST kinase domain-containing protein 4 {ECO:0000303|PubMed:20869947};
DE AltName: Full=Cell cycle progression restoration protein 2;
DE Short=Cell cycle progression protein 2;
DE AltName: Full=Protein TBRG4;
DE AltName: Full=Transforming growth factor beta regulator 4 {ECO:0000312|HGNC:HGNC:17443};
DE Flags: Precursor;
GN Name=TBRG4 {ECO:0000312|HGNC:HGNC:17443};
GN Synonyms=CPR2 {ECO:0000303|PubMed:9383053},
GN FASTKD4 {ECO:0000303|PubMed:20869947}, KIAA0948;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [2]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS SER-22 AND
RP LEU-57.
RC TISSUE=Mammary cancer;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung, and Uterus;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 172-615 (ISOFORM 1), AND FUNCTION.
RC TISSUE=Hepatoma;
RX PubMed=9383053; DOI=10.1093/genetics/147.3.1063;
RA Edwards M.C., Liegeois N., Horecka J., DePinho R.A., Sprague G.F. Jr.,
RA Tyers M., Elledge S.J.;
RT "Human CPR (cell cycle progression restoration) genes impart a Far-
RT phenotype on yeast cells.";
RL Genetics 147:1063-1076(1997).
RN [9]
RP TISSUE SPECIFICITY.
RC TISSUE=Lung;
RX PubMed=12759187; DOI=10.1016/s0167-4781(03)00051-4;
RA Rival-Gervier S., Thepot D., Jolivet G., Houdebine L.-M.;
RT "Pig whey acidic protein gene is surrounded by two ubiquitously expressed
RT genes.";
RL Biochim. Biophys. Acta 1627:7-14(2003).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20869947; DOI=10.1016/j.bbrc.2010.09.075;
RA Simarro M., Gimenez-Cassina A., Kedersha N., Lazaro J.B., Adelmant G.O.,
RA Marto J.A., Rhee K., Tisdale S., Danial N., Benarafa C., Orduna A.,
RA Anderson P.;
RT "Fast kinase domain-containing protein 3 is a mitochondrial protein
RT essential for cellular respiration.";
RL Biochem. Biophys. Res. Commun. 401:440-446(2010).
RN [13]
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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-553, AND IDENTIFICATION BY
RP 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 [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [17]
RP SUBCELLULAR LOCATION, FUNCTION, DOMAIN, AND MUTAGENESIS OF ASP-531.
RX PubMed=28335001; DOI=10.1093/nar/gkx164;
RA Boehm E., Zaganelli S., Maundrell K., Jourdain A.A., Thore S.,
RA Martinou J.C.;
RT "FASTKD1 and FASTKD4 have opposite effects on expression of specific
RT mitochondrial RNAs, depending upon their endonuclease-like RAP domain.";
RL Nucleic Acids Res. 45:6135-6146(2017).
CC -!- FUNCTION: Plays a role in processing of mitochondrial RNA precursors
CC and in stabilization of a subset of mature mitochondrial RNA species,
CC such as MT-CO1, MT-CO2, MT-CYB, MT-CO3, MT-ND3, MT-ND5 and MT-ATP8/6.
CC May play a role in cell cycle progression (PubMed:9383053).
CC {ECO:0000269|PubMed:28335001, ECO:0000269|PubMed:9383053}.
CC -!- INTERACTION:
CC Q969Z0; Q6RW13: AGTRAP; NbExp=3; IntAct=EBI-702328, EBI-741181;
CC Q969Z0; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-702328, EBI-11522760;
CC Q969Z0; Q8TD16-2: BICD2; NbExp=3; IntAct=EBI-702328, EBI-11975051;
CC Q969Z0; Q8WZ55: BSND; NbExp=3; IntAct=EBI-702328, EBI-7996695;
CC Q969Z0; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-702328, EBI-739580;
CC Q969Z0; Q86X02: CDR2L; NbExp=3; IntAct=EBI-702328, EBI-11063830;
CC Q969Z0; Q8IZR5-2: CMTM4; NbExp=3; IntAct=EBI-702328, EBI-17278014;
CC Q969Z0; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-702328, EBI-11522780;
CC Q969Z0; Q9NRY5: FAM114A2; NbExp=4; IntAct=EBI-702328, EBI-10973142;
CC Q969Z0; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-702328, EBI-10175124;
CC Q969Z0; Q96D09: GPRASP2; NbExp=3; IntAct=EBI-702328, EBI-473189;
CC Q969Z0; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-702328, EBI-18053395;
CC Q969Z0; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-702328, EBI-3044087;
CC Q969Z0; Q9H400: LIME1; NbExp=3; IntAct=EBI-702328, EBI-2830566;
CC Q969Z0; Q969L2: MAL2; NbExp=3; IntAct=EBI-702328, EBI-944295;
CC Q969Z0; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-702328, EBI-16439278;
CC Q969Z0; Q04118: PRB3; NbExp=3; IntAct=EBI-702328, EBI-13360404;
CC Q969Z0; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-702328, EBI-10192441;
CC Q969Z0; O15126: SCAMP1; NbExp=3; IntAct=EBI-702328, EBI-954338;
CC Q969Z0; Q8WV19: SFT2D1; NbExp=3; IntAct=EBI-702328, EBI-2854842;
CC Q969Z0; B7ZLI8: STK19; NbExp=3; IntAct=EBI-702328, EBI-10176124;
CC Q969Z0; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-702328, EBI-1105213;
CC Q969Z0; Q8WW34-2: TMEM239; NbExp=3; IntAct=EBI-702328, EBI-11528917;
CC Q969Z0; Q9UBN6: TNFRSF10D; NbExp=3; IntAct=EBI-702328, EBI-1044859;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:20869947, ECO:0000269|PubMed:28335001}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q969Z0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q969Z0-2; Sequence=VSP_022460;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed (PubMed:12759187).
CC Expression detected in spleen, thymus, testis, ovary, colon, heart,
CC smooth muscle, kidney, brain, lung, liver and white adipose tissue with
CC highest expression in smooth muscle (PubMed:20869947).
CC {ECO:0000269|PubMed:12759187, ECO:0000269|PubMed:20869947}.
CC -!- DOMAIN: RAP domain is required for TBRG4 function in mRNA stability and
CC translation. {ECO:0000269|PubMed:28335001}.
CC -!- SIMILARITY: Belongs to the FAST kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB69312.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA76792.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB023165; BAA76792.2; ALT_INIT; mRNA.
DR EMBL; AK222943; BAD96663.1; -; mRNA.
DR EMBL; AL833840; CAD38700.1; -; mRNA.
DR EMBL; CH236960; EAL23744.1; -; Genomic_DNA.
DR EMBL; CH236960; EAL23745.1; -; Genomic_DNA.
DR EMBL; CH471128; EAW61051.1; -; Genomic_DNA.
DR EMBL; CH471128; EAW61052.1; -; Genomic_DNA.
DR EMBL; CH471128; EAW61054.1; -; Genomic_DNA.
DR EMBL; CH471128; EAW61055.1; -; Genomic_DNA.
DR EMBL; BC002732; AAH02732.2; -; mRNA.
DR EMBL; BC014918; AAH14918.1; -; mRNA.
DR EMBL; BC017235; AAH17235.1; -; mRNA.
DR EMBL; AF011792; AAB69312.1; ALT_FRAME; mRNA.
DR CCDS; CCDS5501.1; -. [Q969Z0-1]
DR CCDS; CCDS5502.1; -. [Q969Z0-2]
DR RefSeq; NP_004740.2; NM_004749.3. [Q969Z0-1]
DR RefSeq; NP_112162.1; NM_030900.3. [Q969Z0-2]
DR RefSeq; NP_954573.1; NM_199122.2. [Q969Z0-2]
DR AlphaFoldDB; Q969Z0; -.
DR SMR; Q969Z0; -.
DR BioGRID; 114666; 408.
DR IntAct; Q969Z0; 63.
DR MINT; Q969Z0; -.
DR STRING; 9606.ENSP00000258770; -.
DR GlyGen; Q969Z0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q969Z0; -.
DR MetOSite; Q969Z0; -.
DR PhosphoSitePlus; Q969Z0; -.
DR BioMuta; TBRG4; -.
DR DMDM; 74731072; -.
DR EPD; Q969Z0; -.
DR jPOST; Q969Z0; -.
DR MassIVE; Q969Z0; -.
DR MaxQB; Q969Z0; -.
DR PaxDb; Q969Z0; -.
DR PeptideAtlas; Q969Z0; -.
DR PRIDE; Q969Z0; -.
DR ProteomicsDB; 75880; -. [Q969Z0-1]
DR ProteomicsDB; 75881; -. [Q969Z0-2]
DR Antibodypedia; 13534; 185 antibodies from 28 providers.
DR DNASU; 9238; -.
DR Ensembl; ENST00000258770.8; ENSP00000258770.3; ENSG00000136270.14. [Q969Z0-1]
DR Ensembl; ENST00000361278.7; ENSP00000354992.3; ENSG00000136270.14. [Q969Z0-2]
DR Ensembl; ENST00000395655.8; ENSP00000379016.4; ENSG00000136270.14. [Q969Z0-2]
DR Ensembl; ENST00000494076.5; ENSP00000420597.1; ENSG00000136270.14. [Q969Z0-1]
DR GeneID; 9238; -.
DR KEGG; hsa:9238; -.
DR MANE-Select; ENST00000258770.8; ENSP00000258770.3; NM_004749.4; NP_004740.2.
DR UCSC; uc003tmv.5; human. [Q969Z0-1]
DR CTD; 9238; -.
DR DisGeNET; 9238; -.
DR GeneCards; TBRG4; -.
DR HGNC; HGNC:17443; TBRG4.
DR HPA; ENSG00000136270; Low tissue specificity.
DR MIM; 611325; gene.
DR neXtProt; NX_Q969Z0; -.
DR OpenTargets; ENSG00000136270; -.
DR PharmGKB; PA134882196; -.
DR VEuPathDB; HostDB:ENSG00000136270; -.
DR eggNOG; ENOG502QTRE; Eukaryota.
DR GeneTree; ENSGT01030000234607; -.
DR HOGENOM; CLU_029448_0_0_1; -.
DR InParanoid; Q969Z0; -.
DR OMA; EPVFTPY; -.
DR PhylomeDB; Q969Z0; -.
DR TreeFam; TF324885; -.
DR PathwayCommons; Q969Z0; -.
DR SignaLink; Q969Z0; -.
DR BioGRID-ORCS; 9238; 45 hits in 1082 CRISPR screens.
DR ChiTaRS; TBRG4; human.
DR GeneWiki; TBRG4; -.
DR GenomeRNAi; 9238; -.
DR Pharos; Q969Z0; Tbio.
DR PRO; PR:Q969Z0; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q969Z0; protein.
DR Bgee; ENSG00000136270; Expressed in mucosa of transverse colon and 129 other tissues.
DR ExpressionAtlas; Q969Z0; baseline and differential.
DR Genevisible; Q969Z0; HS.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0035770; C:ribonucleoprotein granule; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0090615; P:mitochondrial mRNA processing; IMP:UniProtKB.
DR GO; GO:0000963; P:mitochondrial RNA processing; IBA:GO_Central.
DR GO; GO:0016071; P:mRNA metabolic process; IMP:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; TAS:UniProtKB.
DR GO; GO:0044528; P:regulation of mitochondrial mRNA stability; IMP:UniProtKB.
DR InterPro; IPR013579; FAST_2.
DR InterPro; IPR010622; FAST_Leu-rich.
DR InterPro; IPR013584; RAP.
DR Pfam; PF06743; FAST_1; 1.
DR Pfam; PF08368; FAST_2; 1.
DR Pfam; PF08373; RAP; 1.
DR SMART; SM00952; RAP; 1.
DR PROSITE; PS51286; RAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Mitochondrion; Phosphoprotein; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..107
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 108..631
FT /note="FAST kinase domain-containing protein 4"
FT /id="PRO_0000273026"
FT DOMAIN 561..619
FT /note="RAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00619"
FT MOD_RES 553
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 246..355
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10231032, ECO:0000303|Ref.3"
FT /id="VSP_022460"
FT VARIANT 22
FT /note="A -> S (in dbSNP:rs2304694)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_030071"
FT VARIANT 57
FT /note="P -> L (in dbSNP:rs2304693)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_030072"
FT MUTAGEN 531
FT /note="D->A: Does not affect location in mitochondria;
FT fails to rescue the increased accumulation of the level of
FT mature MT-ND3, MT-CO3, MT-CYB or MT-ND5 mRNA in TBRG4-
FT deficient cells; does not abolish the accumulation of the
FT MT-ND5-CYB precursor RNA in a TBRG4-deficient cell line."
FT /evidence="ECO:0000269|PubMed:28335001"
FT CONFLICT 365
FT /note="T -> A (in Ref. 3; BAD96663)"
FT /evidence="ECO:0000305"
FT CONFLICT 489
FT /note="V -> E (in Ref. 8; AAB69312)"
FT /evidence="ECO:0000305"
FT CONFLICT 524
FT /note="A -> S (in Ref. 8; AAB69312)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 631 AA; 70738 MW; 4EFC3AF5D5BBABD3 CRC64;
MAAHLVKRCT CLLREAARQA PAMAPVGRLR LAWVAHKTLT SSATSPISHL PGSLMEPVEK
ERASTPYIEK QVDHLIKKAT RPEELLELLG GSHDLDSNQA AMVLIRLSHL LSEKPEDKGL
LIQDAHFHQL LCLLNSQIAS VWHGTLSKLL GSLYALGIPK ASKELQSVEQ EVRWRMRKLK
YKHLAFLAES CATLSQEQHS QELLAELLTH LERRWTEIED SHTLVTVMMK VGHLSEPLMN
RLEDKCLELV EHFGPNELRK VLVMLAAQSR RSVPLLRAIS YHLVQKPFSL TKDVLLDVAY
AYGKLSFHQT QVSQRLATDL LSLMPSLTSG EVAHCAKSFA LLKWLSLPLF EAFAQHVLNR
AQDITLPHLC SVLLAFARLN FHPDQEDQFF SLVHEKLGSE LPGLEPALQV DLVWALCVLQ
QAREAELQAV LHPEFHIQFL GGKSQKDQNT FQKLLHINAT ALLEYPEYSG PLLPASAVAP
GPSALDRKVT PLQKELQETL KGLLGSADKG SLEVATQYGW VLDAEVLLDS DGEFLPVRDF
VAPHLAQPTG SQSPPPGSKR LAFLRWEFPN FNSRSKDLLG RFVLARRHIV AAGFLIVDVP
FYEWLELKSE WQKGAYLKDK MRKAVAEELA K
