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 27-MAR-2024, entry version 172. 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}, FASTKD4 GN {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}; 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; 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; 417. DR IntAct; Q969Z0; 64. 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 SwissPalm; Q969Z0; -. DR BioMuta; TBRG4; -. DR DMDM; 74731072; -. DR EPD; Q969Z0; -. DR jPOST; Q969Z0; -. DR MassIVE; Q969Z0; -. DR MaxQB; Q969Z0; -. DR PaxDb; 9606-ENSP00000258770; -. DR PeptideAtlas; Q969Z0; -. DR ProteomicsDB; 75880; -. [Q969Z0-1] DR ProteomicsDB; 75881; -. [Q969Z0-2] DR Pumba; Q969Z0; -. DR Antibodypedia; 13534; 203 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 AGR; HGNC:17443; -. 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; NFNHSQV; -. DR OrthoDB; 5347066at2759; -. DR PhylomeDB; Q969Z0; -. DR TreeFam; TF324885; -. DR PathwayCommons; Q969Z0; -. DR Reactome; R-HSA-9837092; FASTK family proteins regulate processing and stability of mitochondrial RNAs. DR SignaLink; Q969Z0; -. DR BioGRID-ORCS; 9238; 49 hits in 1161 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 131 other cell types or tissues. DR ExpressionAtlas; Q969Z0; baseline and differential. DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. 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 PANTHER; PTHR21228:SF59; FAST KINASE DOMAIN-CONTAINING PROTEIN 4; 1. DR PANTHER; PTHR21228; FAST LEU-RICH DOMAIN-CONTAINING; 1. 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. DR Genevisible; Q969Z0; HS. 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 FT TBRG4-deficient cells; does not abolish the accumulation of FT the MT-ND5-CYB precursor RNA in a TBRG4-deficient cell FT 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 //