ID   MYG1_HUMAN              Reviewed;         376 AA.
AC   Q9HB07; Q86UA3;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2024, sequence version 4.
DT   27-MAR-2024, entry version 161.
DE   RecName: Full=MYG1 exonuclease {ECO:0000305};
DE            EC=3.1.-.- {ECO:0000303|PubMed:31081026};
DE   Flags: Precursor;
GN   Name=MYG1 {ECO:0000312|HGNC:HGNC:17590}; Synonyms=C12orf10;
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].
RA   Smicun Y.;
RT   "The human homologue of MYG1 the highly conserved gene from autonomously
RT   proliferating mouse melanocytes.";
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA   Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA   Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA   Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA   Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA   Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA   Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA   Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA   Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA   Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA   Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA   Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA   Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA   David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA   D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA   Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA   Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA   Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA   LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA   Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA   Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA   Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA   Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA   Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA   Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA   Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA   Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA   Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA   Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA   Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [3]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000312|EMBL:AAH51871.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain {ECO:0000312|EMBL:AAH51871.1};
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   TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=19014353; DOI=10.1042/bc20080086;
RA   Philips M.-A., Vikesaa J., Luuk H., Joenson L., Lillevaeli K.,
RA   Rehfeld J.F., Vasar E., Koks S., Nielsen F.C.;
RT   "Characterization of MYG1 gene and protein: subcellular distribution and
RT   function.";
RL   Biol. Cell 101:361-373(2009).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-267, AND IDENTIFICATION BY MASS
RP   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   [7]
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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
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   [9]
RP   FUNCTION, MUTAGENESIS OF 106-ASP--HIS-108 AND HIS-344, AND INVOLVEMENT IN
RP   VITILIGO.
RX   PubMed=31081026; DOI=10.1093/nar/gkz371;
RA   Grover R., Burse S.A., Shankrit S., Aggarwal A., Kirty K., Narta K.,
RA   Srivastav R., Ray A.K., Malik G., Vats A., Motiani R.K., Thukral L.,
RA   Roy S.S., Bhattacharya S., Sharma R., Natarajan K., Mukerji M., Pandey R.,
RA   Gokhale R.S., Natarajan V.T.;
RT   "Myg1 exonuclease couples the nuclear and mitochondrial translational
RT   programs through RNA processing.";
RL   Nucleic Acids Res. 47:5852-5866(2019).
RN   [10]
RP   INVOLVEMENT IN VITILIGO, VARIANT GLN-4, CHARACTERIZATION OF VARIANT GLN-4,
RP   AND SUBCELLULAR LOCATION.
RX   PubMed=20377893; DOI=10.1186/1471-2350-11-56;
RA   Philips M.A., Kingo K., Karelson M., Raetsep R., Aunin E., Reimann E.,
RA   Reemann P., Porosaar O., Vikesaa J., Nielsen F.C., Vasar E., Silm H.,
RA   Koks S.;
RT   "Promoter polymorphism -119C/G in MYG1 (C12orf10) gene is related to
RT   vitiligo susceptibility and Arg4Gln affects mitochondrial entrance of
RT   Myg1.";
RL   BMC Med. Genet. 11:56-56(2010).
RN   [11]
RP   INVOLVEMENT IN VITILIGO.
RX   PubMed=30051642; DOI=10.1111/jdv.15195;
RA   Traks T., Keermann M., Karelson M., Raetsep R., Reimann E., Silm H.,
RA   Vasar E., Koks S., Kingo K.;
RT   "Polymorphisms in melanocortin system and MYG1 genes are associated with
RT   vitiligo.";
RL   J. Eur. Acad. Dermatol. Venereol. 33:e65-e67(2019).
CC   -!- FUNCTION: 3'-5' RNA exonuclease which cleaves in situ on specific
CC       transcripts in both nucleus and mitochondrion. Involved in regulating
CC       spatially segregated organellar RNA processing, acts as a coordinator
CC       of nucleo-mitochondrial crosstalk (PubMed:31081026). In nucleolus,
CC       processes pre-ribosomal RNA involved in ribosome assembly and alters
CC       cytoplasmic translation. In mitochondrial matrix, processes 3'-termini
CC       of the mito-ribosomal and messenger RNAs and controls translation of
CC       mitochondrial proteins (Probable). {ECO:0000269|PubMed:31081026,
CC       ECO:0000305|PubMed:31081026}.
CC   -!- INTERACTION:
CC       Q9HB07; Q6RW13: AGTRAP; NbExp=4; IntAct=EBI-709754, EBI-741181;
CC       Q9HB07; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-709754, EBI-11522760;
CC       Q9HB07; P49419-2: ALDH7A1; NbExp=3; IntAct=EBI-709754, EBI-11107920;
CC       Q9HB07; Q10567-3: AP1B1; NbExp=3; IntAct=EBI-709754, EBI-11978055;
CC       Q9HB07; Q6Q788: APOA5; NbExp=3; IntAct=EBI-709754, EBI-3936819;
CC       Q9HB07; Q15041: ARL6IP1; NbExp=6; IntAct=EBI-709754, EBI-714543;
CC       Q9HB07; Q8WZ55: BSND; NbExp=3; IntAct=EBI-709754, EBI-7996695;
CC       Q9HB07; Q9BSJ5: C17orf80; NbExp=3; IntAct=EBI-709754, EBI-2872520;
CC       Q9HB07; O95674: CDS2; NbExp=3; IntAct=EBI-709754, EBI-3913685;
CC       Q9HB07; Q96DZ9: CMTM5; NbExp=4; IntAct=EBI-709754, EBI-2548702;
CC       Q9HB07; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-709754, EBI-11522780;
CC       Q9HB07; Q6PUV4: CPLX2; NbExp=3; IntAct=EBI-709754, EBI-2689453;
CC       Q9HB07; Q9UHG0: DCDC2; NbExp=3; IntAct=EBI-709754, EBI-10303987;
CC       Q9HB07; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-709754, EBI-742054;
CC       Q9HB07; Q9BSY9: DESI2; NbExp=3; IntAct=EBI-709754, EBI-12878374;
CC       Q9HB07; Q6ZPD8: DGAT2L6; NbExp=3; IntAct=EBI-709754, EBI-12831978;
CC       Q9HB07; P26641: EEF1G; NbExp=3; IntAct=EBI-709754, EBI-351467;
CC       Q9HB07; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-709754, EBI-781551;
CC       Q9HB07; Q8IZU0: FAM9B; NbExp=4; IntAct=EBI-709754, EBI-10175124;
CC       Q9HB07; Q8TAE8: GADD45GIP1; NbExp=3; IntAct=EBI-709754, EBI-372506;
CC       Q9HB07; P62993: GRB2; NbExp=3; IntAct=EBI-709754, EBI-401755;
CC       Q9HB07; Q86X24: HORMAD1; NbExp=3; IntAct=EBI-709754, EBI-12165207;
CC       Q9HB07; Q969L2: MAL2; NbExp=3; IntAct=EBI-709754, EBI-944295;
CC       Q9HB07; Q9NR34: MAN1C1; NbExp=3; IntAct=EBI-709754, EBI-7260764;
CC       Q9HB07; Q9H1A3: METTL9; NbExp=3; IntAct=EBI-709754, EBI-2804879;
CC       Q9HB07; Q9BRX2: PELO; NbExp=3; IntAct=EBI-709754, EBI-1043580;
CC       Q9HB07; O60664: PLIN3; NbExp=3; IntAct=EBI-709754, EBI-725795;
CC       Q9HB07; Q59EV6: PPGB; NbExp=3; IntAct=EBI-709754, EBI-14210385;
CC       Q9HB07; P57052: RBM11; NbExp=3; IntAct=EBI-709754, EBI-741332;
CC       Q9HB07; Q96HR9-2: REEP6; NbExp=3; IntAct=EBI-709754, EBI-14065960;
CC       Q9HB07; Q6NTF9-3: RHBDD2; NbExp=3; IntAct=EBI-709754, EBI-17589229;
CC       Q9HB07; Q03395: ROM1; NbExp=3; IntAct=EBI-709754, EBI-9395257;
CC       Q9HB07; P28702: RXRB; NbExp=3; IntAct=EBI-709754, EBI-748576;
CC       Q9HB07; Q8WV19: SFT2D1; NbExp=3; IntAct=EBI-709754, EBI-2854842;
CC       Q9HB07; Q9BYT1: SLC17A9; NbExp=3; IntAct=EBI-709754, EBI-3940816;
CC       Q9HB07; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-709754, EBI-742688;
CC       Q9HB07; O43759-2: SYNGR1; NbExp=3; IntAct=EBI-709754, EBI-12187159;
CC       Q9HB07; P08247: SYP; NbExp=3; IntAct=EBI-709754, EBI-9071725;
CC       Q9HB07; O60830: TIMM17B; NbExp=3; IntAct=EBI-709754, EBI-2372529;
CC       Q9HB07; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-709754, EBI-12947623;
CC       Q9HB07; Q8NBD8: TMEM229B; NbExp=3; IntAct=EBI-709754, EBI-12195227;
CC       Q9HB07; Q8WW34: TMEM239; NbExp=3; IntAct=EBI-709754, EBI-9675724;
CC       Q9HB07; Q9H2S6-2: TNMD; NbExp=3; IntAct=EBI-709754, EBI-12003398;
CC       Q9HB07; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-709754, EBI-12040603;
CC       Q9HB07; O95070: YIF1A; NbExp=3; IntAct=EBI-709754, EBI-2799703;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC       {ECO:0000269|PubMed:19014353, ECO:0000269|PubMed:20377893}.
CC       Mitochondrion matrix {ECO:0000269|PubMed:19014353,
CC       ECO:0000269|PubMed:20377893}. Nucleus, nucleolus
CC       {ECO:0000250|UniProtKB:Q9JK81}.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
CC       testis. {ECO:0000269|PubMed:19014353}.
CC   -!- DISEASE: Note=Several works have found that mRNA expression is elevated
CC       in the skin of vitiligo patients. {ECO:0000269|PubMed:20377893,
CC       ECO:0000269|PubMed:30051642, ECO:0000269|PubMed:31081026}.
CC   -!- SIMILARITY: Belongs to the MYG1 family. {ECO:0000305}.
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DR   EMBL; AF289485; AAG17847.1; -; mRNA.
DR   EMBL; AC073611; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471054; EAW96688.1; -; Genomic_DNA.
DR   EMBL; BC051871; AAH51871.1; -; mRNA.
DR   CCDS; CCDS31810.1; -.
DR   RefSeq; NP_067653.3; NM_021640.3.
DR   AlphaFoldDB; Q9HB07; -.
DR   IntAct; Q9HB07; 50.
DR   MINT; Q9HB07; -.
DR   STRING; 9606.ENSP00000267103; -.
DR   GlyGen; Q9HB07; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9HB07; -.
DR   MetOSite; Q9HB07; -.
DR   PhosphoSitePlus; Q9HB07; -.
DR   SwissPalm; Q9HB07; -.
DR   BioMuta; C12orf10; -.
DR   DMDM; 296439232; -.
DR   REPRODUCTION-2DPAGE; IPI00029444; -.
DR   EPD; Q9HB07; -.
DR   jPOST; Q9HB07; -.
DR   MassIVE; Q9HB07; -.
DR   MaxQB; Q9HB07; -.
DR   PaxDb; 9606-ENSP00000267103; -.
DR   PeptideAtlas; Q9HB07; -.
DR   ProteomicsDB; 81466; -.
DR   Pumba; Q9HB07; -.
DR   Antibodypedia; 48361; 46 antibodies from 12 providers.
DR   DNASU; 60314; -.
DR   Ensembl; ENST00000267103.10; ENSP00000267103.5; ENSG00000139637.14.
DR   Ensembl; ENST00000708949.1; ENSP00000517432.1; ENSG00000291835.1.
DR   GeneID; 60314; -.
DR   KEGG; hsa:60314; -.
DR   MANE-Select; ENST00000267103.10; ENSP00000267103.5; NM_021640.4; NP_067653.4.
DR   UCSC; uc001scp.5; human.
DR   AGR; HGNC:17590; -.
DR   CTD; 60314; -.
DR   GeneCards; MYG1; -.
DR   HGNC; HGNC:17590; MYG1.
DR   HPA; ENSG00000139637; Low tissue specificity.
DR   MIM; 611366; gene.
DR   neXtProt; NX_Q9HB07; -.
DR   VEuPathDB; HostDB:ENSG00000139637; -.
DR   eggNOG; KOG2948; Eukaryota.
DR   InParanoid; Q9HB07; -.
DR   OrthoDB; 19907at2759; -.
DR   PhylomeDB; Q9HB07; -.
DR   TreeFam; TF313313; -.
DR   PathwayCommons; Q9HB07; -.
DR   SignaLink; Q9HB07; -.
DR   BioGRID-ORCS; 60314; 45 hits in 1152 CRISPR screens.
DR   ChiTaRS; C12orf10; human.
DR   GenomeRNAi; 60314; -.
DR   Pharos; Q9HB07; Tbio.
DR   PRO; PR:Q9HB07; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; Q9HB07; Protein.
DR   Bgee; ENSG00000139637; Expressed in primary visual cortex and 100 other cell types or tissues.
DR   ExpressionAtlas; Q9HB07; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0035641; P:locomotory exploration behavior; IEA:Ensembl.
DR   InterPro; IPR003226; Met-dep_prot_hydro.
DR   PANTHER; PTHR11215; METAL DEPENDENT HYDROLASE - RELATED; 1.
DR   PANTHER; PTHR11215:SF1; MYG1 EXONUCLEASE; 1.
DR   Pfam; PF03690; UPF0160; 1.
DR   Genevisible; Q9HB07; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Hydrolase; Mitochondrion; Nuclease; Nucleus; Phosphoprotein;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..47
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           48..376
FT                   /note="MYG1 exonuclease"
FT                   /id="PRO_0000213483"
FT   MOD_RES         120
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         267
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         273
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JK81"
FT   VARIANT         4
FT                   /note="R -> Q (loss of mitochondrial location;
FT                   dbSNP:rs1534284)"
FT                   /evidence="ECO:0000269|PubMed:20377893"
FT                   /id="VAR_083553"
FT   VARIANT         349
FT                   /note="I -> T (in dbSNP:rs1534282)"
FT                   /evidence="ECO:0000269|Ref.1"
FT                   /id="VAR_059854"
FT   MUTAGEN         106..108
FT                   /note="DHH->AAL: Catalytically inactive."
FT                   /evidence="ECO:0000269|PubMed:31081026"
FT   MUTAGEN         344
FT                   /note="H->Q: Loss of RNase activity and gained single
FT                   stranded DNase activity."
FT                   /evidence="ECO:0000269|PubMed:31081026"
FT   CONFLICT        150
FT                   /note="T -> P (in Ref. 1; AAG17847)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        353
FT                   /note="R -> P (in Ref. 1; AAG17847)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   376 AA;  42508 MW;  3D7151062EA70C06 CRC64;
     MGHRFLRGLL TLLLPPPPLY TRHRMLGPES VPPPKRSRSK LMAPPRIGTH NGTFHCDEAL
     ACALLRLLPE YRDAEIVRTR DPEKLASCDI VVDVGGEYDP RRHRYDHHQR SFTETMSSLS
     PGKPWQTKLS SAGLIYLHFG HKLLAQLLGT SEEDSMVGTL YDKMYENFVE EVDAVDNGIS
     QWAEGEPRYA LTTTLSARVA RLNPTWNHPD QDTEAGFKRA MDLVQEEFLQ RLDFYQHSWL
     PARALVEEAL AQRFQVDPSG EIVELAKGAC PWKEHLYHLE SGLSPPVAIF FVIYTDQAGQ
     WRIQCVPKEP HSFQSRLPLP EPWRGLRDEA LDQVSGIPGC IFVHASGFIG GHRTREGALS
     MARATLAQRS YLPQIS
//