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DNA helicase MCM9 (hMCM9) (EC 3.6.4.12) (Mini-chromosome maintenance deficient domain-containing protein 1) (Minichromosome maintenance 9)

 MCM9_HUMAN              Reviewed;        1143 AA.
Q9NXL9; B4DR30; B9DI77; Q2KHJ0; Q8N5S5; Q9HCV5;
05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
16-MAY-2012, sequence version 4.
10-OCT-2018, entry version 130.
RecName: Full=DNA helicase MCM9;
Short=hMCM9;
EC=3.6.4.12 {ECO:0000269|PubMed:26300262};
AltName: Full=Mini-chromosome maintenance deficient domain-containing protein 1;
AltName: Full=Minichromosome maintenance 9;
Name=MCM9; Synonyms=C6orf61, MCMDC1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 865-1143 (ISOFORM L).
TISSUE=Teratocarcinoma;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM S).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
IDENTIFICATION.
PubMed=16226853; DOI=10.1016/j.gene.2005.07.031;
Lutzmann M., Maiorano D., Mechali M.;
"Identification of full genes and proteins of MCM9, a novel,
vertebrate-specific member of the MCM2-8 protein family.";
Gene 362:51-56(2005).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-762, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[7]
ALTERNATIVE SPLICING (ISOFORM M), AND DEVELOPMENTAL STAGE.
PubMed=23403237; DOI=10.1016/j.gene.2013.01.054;
Jeffries E.P., Denq W.I., Bartko J.C., Trakselis M.A.;
"Identification, quantification, and evolutionary analysis of a novel
isoform of MCM9.";
Gene 519:41-49(2013).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-762; SER-802 AND
SER-1109, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[9]
FUNCTION, IDENTIFICATION IN THE MCM8-MCM9 COMPLEX, INTERACTION WITH
RAD51, AND SUBCELLULAR LOCATION.
PubMed=23401855; DOI=10.1128/MCB.01503-12;
Park J., Long D.T., Lee K.Y., Abbas T., Shibata E., Negishi M.,
Luo Y., Schimenti J.C., Gambus A., Walter J.C., Dutta A.;
"The MCM8-MCM9 complex promotes RAD51 recruitment at DNA damage sites
to facilitate homologous recombination.";
Mol. Cell. Biol. 33:1632-1644(2013).
[10]
INVOLVEMENT IN ODG4.
PubMed=25480036; DOI=10.1016/j.ajhg.2014.11.002;
Wood-Trageser M.A., Gurbuz F., Yatsenko S.A., Jeffries E.P.,
Kotan L.D., Surti U., Ketterer D.M., Matic J., Chipkin J., Jiang H.,
Trakselis M.A., Topaloglu A.K., Rajkovic A.;
"MCM9 mutations are associated with ovarian failure, short stature,
and chromosomal instability.";
Am. J. Hum. Genet. 95:754-762(2014).
[11]
FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION IN THE MCM8-MCM9 COMPLEX,
INTERACTION WITH MMR COMPLEX, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
LYS-358 AND ARG-482.
PubMed=26300262; DOI=10.1016/j.molcel.2015.07.010;
Traver S., Coulombe P., Peiffer I., Hutchins J.R., Kitzmann M.,
Latreille D., Mechali M.;
"MCM9 Is Required for Mammalian DNA Mismatch Repair.";
Mol. Cell 59:831-839(2015).
[12]
FUNCTION, AND INTERACTION WITH MRN COMPLEX AND MCM8.
PubMed=26215093; DOI=10.1038/ncomms8744;
Lee K.Y., Im J.S., Shibata E., Park J., Handa N., Kowalczykowski S.C.,
Dutta A.;
"MCM8-9 complex promotes resection of double-strand break ends by
MRE11-RAD50-NBS1 complex.";
Nat. Commun. 6:7744-7744(2015).
-!- FUNCTION: Component of the MCM8-MCM9 complex, a complex involved
in the repair of double-stranded DNA breaks (DBSs) and DNA
interstrand cross-links (ICLs) by homologous recombination (HR)
(PubMed:23401855). Required for DNA resection by the MRE11-RAD50-
NBN/NBS1 (MRN) complex by recruiting the MRN complex to the repair
site and by promoting the complex nuclease activity
(PubMed:26215093). Probably by regulating the localization of the
MRN complex, indirectly regulates the recruitment of downstream
effector RAD51 to DNA damage sites including DBSs and ICLs
(PubMed:23401855). Acts as an helicase in DNA mismatch repair
(MMR) following DNA replication errors to unwind the mismatch
containing DNA strand (PubMed:26300262). In addition, recruits
MLH1, a component of the MMR complex, to chromatin
(PubMed:26300262). The MCM8-MCM9 complex is dispensable for DNA
replication and S phase progression (PubMed:23401855). Probably by
regulating HR, plays a key role during gametogenesis (By
similarity). {ECO:0000250|UniProtKB:Q2KHI9,
ECO:0000269|PubMed:23401855, ECO:0000269|PubMed:26215093,
ECO:0000269|PubMed:26300262}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000269|PubMed:26300262}.
-!- SUBUNIT: Component of the MCM8-MCM9 complex, which forms a hexamer
composed of MCM8 and MCM9 (PubMed:23401855, PubMed:26300262,
PubMed:26215093). Interacts with the DNA mismatch repair (MMR)
complex composed at least of MSH2, MSH3, MSH6, PMS1 and MLH1
(PubMed:26300262). Interacts with MLH1; the interaction recruits
MLH1 to chromatin (PubMed:26300262). Interacts with MSH2; the
interaction recruits MCM9 to chromatin (PubMed:26300262).
Interacts with MSH6 (PubMed:26300262). Interacts with the MRN
complex composed of MRE11, RAD50 and NBN/NBS1; the interaction
recruits the MRN complex to DNA damage sites (PubMed:26215093).
Interacts with RAD51; the interaction recruits RAD51 to DNA damage
sites (PubMed:23401855). {ECO:0000269|PubMed:23401855,
ECO:0000269|PubMed:26215093, ECO:0000269|PubMed:26300262}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23401855,
ECO:0000269|PubMed:26300262}. Chromosome
{ECO:0000269|PubMed:23401855, ECO:0000269|PubMed:26300262}.
Note=Colocalizes to nuclear foci with RPA1 following DNA damage
(PubMed:23401855). Localizes to double-stranded DNA breaks
(PubMed:23401855). Recruited to chromatin by MSH2
(PubMed:26300262). {ECO:0000269|PubMed:23401855,
ECO:0000269|PubMed:26300262}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=L;
IsoId=Q9NXL9-1; Sequence=Displayed;
Note=Most abundant isoform.;
Name=M;
IsoId=Q9NXL9-2; Sequence=VSP_047462, VSP_047463;
Name=S;
IsoId=Q9NXL9-3; Sequence=VSP_028013, VSP_028014;
Name=4;
IsoId=Q9NXL9-4; Sequence=VSP_044180, VSP_044181;
Note=No experimental confirmation available.;
-!- DEVELOPMENTAL STAGE: The expression of isoform L and isoform M is
cell cycle regulated: induced in S-phase, decreases through G2/M,
and becomes constant through G1. {ECO:0000269|PubMed:23403237}.
-!- DISEASE: Ovarian dysgenesis 4 (ODG4) [MIM:616185]: A disorder
characterized by lack of spontaneous pubertal development, primary
amenorrhea, uterine hypoplasia, and hypergonadotropic hypogonadism
as a result of streak gonads. {ECO:0000269|PubMed:25480036}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA90991.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAG61142.1; Type=Erroneous termination; Positions=1070; Note=Translated as Lys.; Evidence={ECO:0000305};
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EMBL; AK299076; BAG61142.1; ALT_SEQ; mRNA.
EMBL; AK000177; BAA90991.1; ALT_INIT; mRNA.
EMBL; AL132874; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL359634; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC031658; AAH31658.1; -; mRNA.
EMBL; BN000882; CAJ70648.1; -; mRNA.
CCDS; CCDS5121.1; -. [Q9NXL9-3]
CCDS; CCDS56447.1; -. [Q9NXL9-1]
RefSeq; NP_060166.2; NM_017696.2. [Q9NXL9-1]
RefSeq; NP_694987.1; NM_153255.4. [Q9NXL9-3]
UniGene; Hs.279008; -.
UniGene; Hs.733116; -.
UniGene; Hs.736853; -.
ProteinModelPortal; Q9NXL9; -.
SMR; Q9NXL9; -.
BioGrid; 129033; 37.
IntAct; Q9NXL9; 3.
STRING; 9606.ENSP00000314505; -.
iPTMnet; Q9NXL9; -.
PhosphoSitePlus; Q9NXL9; -.
BioMuta; MCM9; -.
DMDM; 387912921; -.
EPD; Q9NXL9; -.
MaxQB; Q9NXL9; -.
PaxDb; Q9NXL9; -.
PeptideAtlas; Q9NXL9; -.
PRIDE; Q9NXL9; -.
ProteomicsDB; 83112; -.
ProteomicsDB; 83113; -. [Q9NXL9-2]
DNASU; 254394; -.
Ensembl; ENST00000316068; ENSP00000312870; ENSG00000111877. [Q9NXL9-3]
Ensembl; ENST00000316316; ENSP00000314505; ENSG00000111877. [Q9NXL9-1]
Ensembl; ENST00000619706; ENSP00000480469; ENSG00000111877. [Q9NXL9-1]
GeneID; 254394; -.
KEGG; hsa:254394; -.
UCSC; uc003pyh.4; human. [Q9NXL9-1]
CTD; 254394; -.
DisGeNET; 254394; -.
EuPathDB; HostDB:ENSG00000111877.17; -.
GeneCards; MCM9; -.
HGNC; HGNC:21484; MCM9.
HPA; HPA031137; -.
MalaCards; MCM9; -.
MIM; 610098; gene.
MIM; 616185; phenotype.
neXtProt; NX_Q9NXL9; -.
OpenTargets; ENSG00000111877; -.
PharmGKB; PA162395071; -.
eggNOG; KOG0477; Eukaryota.
eggNOG; COG1241; LUCA.
GeneTree; ENSGT00920000149094; -.
HOGENOM; HOG000007282; -.
HOVERGEN; HBG108122; -.
InParanoid; Q9NXL9; -.
KO; K10738; -.
OMA; VMCAPEK; -.
OrthoDB; EOG091G01CK; -.
PhylomeDB; Q9NXL9; -.
TreeFam; TF329421; -.
ChiTaRS; MCM9; human.
GenomeRNAi; 254394; -.
PRO; PR:Q9NXL9; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000111877; Expressed in 175 organ(s), highest expression level in secondary oocyte.
CleanEx; HS_MCM9; -.
ExpressionAtlas; Q9NXL9; baseline and differential.
Genevisible; Q9NXL9; HS.
GO; GO:0097362; C:MCM8-MCM9 complex; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA:UniProtKB.
GO; GO:0007292; P:female gamete generation; ISS:UniProtKB.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR031327; MCM.
InterPro; IPR001208; MCM_dom.
InterPro; IPR033762; MCM_OB.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR11630; PTHR11630; 1.
Pfam; PF00493; MCM; 1.
Pfam; PF17207; MCM_OB; 1.
PRINTS; PR01657; MCMFAMILY.
SMART; SM00382; AAA; 1.
SMART; SM00350; MCM; 1.
SUPFAM; SSF50249; SSF50249; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50051; MCM_2; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Chromosome; Complete proteome;
DNA damage; DNA repair; DNA-binding; Helicase; Hydrolase;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
CHAIN 1 1143 DNA helicase MCM9.
/FTId=PRO_0000089513.
DOMAIN 300 505 MCM. {ECO:0000255}.
NP_BIND 352 359 ATP. {ECO:0000255}.
MOD_RES 762 762 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 802 802 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1109 1109 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 381 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044180.
VAR_SEQ 382 383 SA -> MS (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044181.
VAR_SEQ 383 391 AGLTVTAVK -> AGIVCDNFK (in isoform S).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_028013.
VAR_SEQ 392 1143 Missing (in isoform S).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_028014.
VAR_SEQ 606 648 GGALLGGVNALHTSFPENPGEQYQRQCELILEKLELQSLLS
EE -> VTESECAPIPTTGIGGRDYSRILEKWSRGRIKLQN
FITAGNQL (in isoform M). {ECO:0000305}.
/FTId=VSP_047462.
VAR_SEQ 649 1143 Missing (in isoform M). {ECO:0000305}.
/FTId=VSP_047463.
MUTAGEN 358 358 K->A: Loss of helicase activity and DNA
mismatch repair function but does not
affect the interaction with MCM8, MSH2 or
chromatin; when associated with A-482.
{ECO:0000269|PubMed:26300262}.
MUTAGEN 482 482 R->A: Loss of helicase activity and DNA
mismatch repair function but does not
affect the interaction with MCM8, MSH2 or
chromatin; when associated with A-358.
{ECO:0000269|PubMed:26300262}.
CONFLICT 433 433 Q -> R (in Ref. 1; BAG61142).
{ECO:0000305}.
CONFLICT 558 558 C -> S (in Ref. 1; BAG61142).
{ECO:0000305}.
CONFLICT 1063 1063 F -> V (in Ref. 1; BAA90991).
{ECO:0000305}.
CONFLICT 1136 1136 D -> G (in Ref. 1; BAA90991).
{ECO:0000305}.
SEQUENCE 1143 AA; 127313 MW; 3C35C8B3476A470F CRC64;
MNSDQVTLVG QVFESYVSEY HKNDILLILK ERDEDAHYPV VVNAMTLFET NMEIGEYFNM
FPSEVLTIFD SALRRSALTI LQSLSQPEAV SMKQNLHARI SGLPVCPELV REHIPKTKDV
GHFLSVTGTV IRTSLVKVLE FERDYMCNKC KHVFVIKADF EQYYTFCRPS SCPSLESCDS
SKFTCLSGLS SSPTRCRDYQ EIKIQEQVQR LSVGSIPRSM KVILEDDLVD SCKSGDDLTI
YGIVMQRWKP FQQDVRCEVE IVLKANYIQV NNEQSSGIIM DEEVQKEFED FWEYYKSDPF
AGRNVILASL CPQVFGMYLV KLAVAMVLAG GIQRTDATGT RVRGESHLLL VGDPGTGKSQ
FLKYAAKITP RSVLTTGIGS TSAGLTVTAV KDSGEWNLEA GALVLADAGL CCIDEFNSLK
EHDRTSIHEA MEQQTISVAK AGLVCKLNTR TTILAATNPK GQYDPQESVS VNIALGSPLL
SRFDLILVLL DTKNEDWDRI ISSFILENKG YPSKSEKLWS MEKMKTYFCL IRNLQPTLSD
VGNQVLLRYY QMQRQSDCRN AARTTIRLLE SLIRLAEAHA RLMFRDTVTL EDAITVVSVM
ESSMQGGALL GGVNALHTSF PENPGEQYQR QCELILEKLE LQSLLSEELR RLERLQNQSV
HQSQPRVLEV ETTPGSLRNG PGEESNFRTS SQQEINYSTH IFSPGGSPEG SPVLDPPPHL
EPNRSTSRKH SAQHKNNRDD SLDWFDFMAT HQSEPKNTVV VSPHPKTSGE NMASKISNST
SQGKEKSEPG QRSKVDIGLL PSPGETGVPW RADNVESNKK KRLALDSEAA VSADKPDSVL
THHVPRNLQK LCKERAQKLC RNSTRVPAQC TVPSHPQSTP VHSPDRMLDS PKRKRPKSLA
QVEEPAIENV KPPGSPVAKL AKFTFKQKSK LIHSFEDHSH VSPGATKIAV HSPKISQRRT
RRDAALPVKR PGKLTSTPGN QISSQPQGET KEVSQQPPEK HGPREKVMCA PEKRIIQPEL
ELGNETGCAH LTCEGDKKEE VSGSNKSGKV HACTLARLAN FCFTPPSESK SKSPPPERKN
RGERGPSSPP TTTAPMRVSK RKSFQLRGST EKLIVSKESL FTLPELGDEA FDCDWDEEMR
KKS


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