M10L1_HUMAN
ID M10L1_HUMAN Reviewed; 1211 AA.
AC Q9BXT6; A7E211; A8MXC6; B7WPP1; B7Z7R1; F5H403; Q5TGD5; Q8NBD4; Q9NXW3;
AC Q9UFB3; Q9UGX9;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=RNA helicase Mov10l1 {ECO:0000305};
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:Q99MV5};
DE AltName: Full=Moloney leukemia virus 10-like protein 1 {ECO:0000312|HGNC:HGNC:7201};
DE Short=MOV10-like protein 1 {ECO:0000312|HGNC:HGNC:7201};
GN Name=MOV10L1 {ECO:0000312|HGNC:HGNC:7201};
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 (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=11279525; DOI=10.1038/86927;
RA Wang P.J., McCarrey J.R., Yang F., Page D.C.;
RT "An abundance of X-linked genes expressed in spermatogonia.";
RL Nat. Genet. 27:422-426(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 5), AND VARIANT
RP ARG-820.
RC TISSUE=Adipose tissue, Cerebellum, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT LEU-454.
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 534-1211, AND VARIANTS LEU-454;
RP ARG-820 AND GLU-1179.
RC TISSUE=Testis;
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).
CC -!- FUNCTION: ATP-dependent RNA helicase required during spermatogenesis to
CC repress transposable elements and prevent their mobilization, which is
CC essential for germline integrity. Acts via the piRNA metabolic process,
CC which mediates the repression of transposable elements during meiosis
CC by forming complexes composed of piRNAs and Piwi proteins and governs
CC the methylation and subsequent repression of transposons. Involved in
CC the primary piRNA metabolic process. Specifically binds to piRNA
CC precursors and promotes the generation of intermediate piRNA processing
CC fragments that are subsequently loaded to Piwi proteins. Acts via its
CC ATP-dependent RNA helicase activity: displays 5'-3' RNA unwinding
CC activity and probably mediates unwinding and funneling of single-
CC stranded piRNA precursor transcripts to the endonuclease that catalyzes
CC the first cleavage step of piRNA processing to generate piRNA
CC intermediate fragments that are subsequently loaded to Piwi proteins.
CC {ECO:0000250|UniProtKB:Q99MV5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000250|UniProtKB:Q99MV5};
CC -!- SUBUNIT: Interacts with PIWIL1. Interacts with PIWIL2. Interacts with
CC PIWIL4. Interacts with HSPA2. Interacts with PLD6.
CC {ECO:0000250|UniProtKB:Q99MV5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q99MV5}.
CC Note=Component of the meiotic nuage, also named P granule, a germ-cell-
CC specific organelle required to repress transposon activity during
CC meiosis. {ECO:0000250|UniProtKB:Q99MV5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q9BXT6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BXT6-2; Sequence=VSP_003390, VSP_003391;
CC Name=3;
CC IsoId=Q9BXT6-3; Sequence=VSP_010945, VSP_010946, VSP_010947,
CC VSP_010948;
CC Name=4;
CC IsoId=Q9BXT6-4; Sequence=VSP_045413;
CC Name=5;
CC IsoId=Q9BXT6-5; Sequence=VSP_046082, VSP_046083;
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Specifically expressed in testis.
CC {ECO:0000269|PubMed:11279525}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family. SDE3 subfamily.
CC {ECO:0000305}.
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DR EMBL; AF285604; AAK31983.1; -; mRNA.
DR EMBL; AK000033; BAA90895.1; -; mRNA.
DR EMBL; AK090740; BAC03511.1; -; mRNA.
DR EMBL; AK302401; BAH13697.1; -; mRNA.
DR EMBL; CR456466; CAG30352.1; -; mRNA.
DR EMBL; AL022328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL034546; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC150137; AAI50138.1; -; mRNA.
DR EMBL; BC152539; AAI52540.1; -; mRNA.
DR EMBL; AL133068; CAB61391.1; -; mRNA.
DR CCDS; CCDS14084.1; -. [Q9BXT6-1]
DR CCDS; CCDS54541.1; -. [Q9BXT6-4]
DR CCDS; CCDS54542.1; -. [Q9BXT6-5]
DR CCDS; CCDS54543.1; -. [Q9BXT6-2]
DR PIR; T42668; T42668.
DR RefSeq; NP_001157576.1; NM_001164104.1. [Q9BXT6-4]
DR RefSeq; NP_001157577.1; NM_001164105.1. [Q9BXT6-5]
DR RefSeq; NP_001157578.1; NM_001164106.1. [Q9BXT6-2]
DR RefSeq; NP_061868.1; NM_018995.2. [Q9BXT6-1]
DR AlphaFoldDB; Q9BXT6; -.
DR BioGRID; 119963; 5.
DR IntAct; Q9BXT6; 1.
DR STRING; 9606.ENSP00000262794; -.
DR GlyGen; Q9BXT6; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; Q9BXT6; -.
DR PhosphoSitePlus; Q9BXT6; -.
DR BioMuta; MOV10L1; -.
DR DMDM; 22095856; -.
DR EPD; Q9BXT6; -.
DR jPOST; Q9BXT6; -.
DR MassIVE; Q9BXT6; -.
DR PaxDb; Q9BXT6; -.
DR PeptideAtlas; Q9BXT6; -.
DR PRIDE; Q9BXT6; -.
DR ProteomicsDB; 2313; -.
DR ProteomicsDB; 26428; -.
DR ProteomicsDB; 79508; -. [Q9BXT6-1]
DR ProteomicsDB; 79509; -. [Q9BXT6-2]
DR ProteomicsDB; 79510; -. [Q9BXT6-3]
DR Antibodypedia; 14100; 96 antibodies from 20 providers.
DR DNASU; 54456; -.
DR Ensembl; ENST00000262794.10; ENSP00000262794.5; ENSG00000073146.16. [Q9BXT6-1]
DR Ensembl; ENST00000354853.2; ENSP00000346917.2; ENSG00000073146.16. [Q9BXT6-3]
DR Ensembl; ENST00000395852.5; ENSP00000379193.1; ENSG00000073146.16. [Q9BXT6-2]
DR Ensembl; ENST00000395858.7; ENSP00000379199.3; ENSG00000073146.16. [Q9BXT6-4]
DR Ensembl; ENST00000540615.5; ENSP00000438542.1; ENSG00000073146.16. [Q9BXT6-5]
DR Ensembl; ENST00000545383.5; ENSP00000438978.1; ENSG00000073146.16. [Q9BXT6-1]
DR GeneID; 54456; -.
DR KEGG; hsa:54456; -.
DR MANE-Select; ENST00000262794.10; ENSP00000262794.5; NM_018995.3; NP_061868.1.
DR UCSC; uc003bjj.4; human. [Q9BXT6-1]
DR CTD; 54456; -.
DR DisGeNET; 54456; -.
DR GeneCards; MOV10L1; -.
DR HGNC; HGNC:7201; MOV10L1.
DR HPA; ENSG00000073146; Tissue enriched (testis).
DR MIM; 605794; gene.
DR neXtProt; NX_Q9BXT6; -.
DR OpenTargets; ENSG00000073146; -.
DR PharmGKB; PA30909; -.
DR VEuPathDB; HostDB:ENSG00000073146; -.
DR eggNOG; KOG1804; Eukaryota.
DR GeneTree; ENSGT00940000160150; -.
DR HOGENOM; CLU_001666_3_1_1; -.
DR InParanoid; Q9BXT6; -.
DR OMA; VVIWIEN; -.
DR OrthoDB; 286011at2759; -.
DR PhylomeDB; Q9BXT6; -.
DR TreeFam; TF323999; -.
DR PathwayCommons; Q9BXT6; -.
DR Reactome; R-HSA-5601884; PIWI-interacting RNA (piRNA) biogenesis.
DR SignaLink; Q9BXT6; -.
DR BioGRID-ORCS; 54456; 10 hits in 1067 CRISPR screens.
DR ChiTaRS; MOV10L1; human.
DR GenomeRNAi; 54456; -.
DR Pharos; Q9BXT6; Tbio.
DR PRO; PR:Q9BXT6; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9BXT6; protein.
DR Bgee; ENSG00000073146; Expressed in right testis and 94 other tissues.
DR ExpressionAtlas; Q9BXT6; baseline and differential.
DR Genevisible; Q9BXT6; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043186; C:P granule; ISS:UniProtKB.
DR GO; GO:0071546; C:pi-body; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; TAS:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0000287; F:magnesium ion binding; TAS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; ISS:UniProtKB.
DR GO; GO:0043046; P:DNA methylation involved in gamete generation; ISS:UniProtKB.
DR GO; GO:0007281; P:germ cell development; IEP:UniProtKB.
DR GO; GO:0007141; P:male meiosis I; ISS:UniProtKB.
DR GO; GO:0034587; P:piRNA metabolic process; ISS:UniProtKB.
DR GO; GO:0035194; P:post-transcriptional gene silencing by RNA; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEP:UniProtKB.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF13086; AAA_11; 2.
DR Pfam; PF13087; AAA_12; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Cytoplasm; Developmental protein;
KW Helicase; Hydrolase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..1211
FT /note="RNA helicase Mov10l1"
FT /id="PRO_0000080706"
FT REGION 340..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1192..1211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 886..889
FT /note="DEAG box"
FT COMPBIAS 340..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..710
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 770..777
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..902
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_010945"
FT VAR_SEQ 1..873
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_003390"
FT VAR_SEQ 1..32
FT /note="MLSLAAKLVAFFWRTADTPREEAGQLEPELAE -> MSFLPVRSVIGG (in
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046082"
FT VAR_SEQ 874..875
FT /note="GV -> MF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_003391"
FT VAR_SEQ 910..964
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_010946"
FT VAR_SEQ 1074..1082
FT /note="EKIRILLRN -> RPAQARLVL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_010947"
FT VAR_SEQ 1083..1211
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_010948"
FT VAR_SEQ 1109..1154
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045413"
FT VAR_SEQ 1155..1211
FT /note="DPCFGALLEYSITNGVYMGCDLPPALQSLQNCGEGVADPSYPVVPESTGPEK
FT HQEPS -> LWRGGGRPLLPSGARIHRTREASGAQLICSG (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046083"
FT VARIANT 18
FT /note="T -> S (in dbSNP:rs12628964)"
FT /id="VAR_059457"
FT VARIANT 57
FT /note="M -> L (in dbSNP:rs9617066)"
FT /id="VAR_034100"
FT VARIANT 182
FT /note="R -> C (in dbSNP:rs3810971)"
FT /id="VAR_020148"
FT VARIANT 454
FT /note="I -> L (in dbSNP:rs760749)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_013694"
FT VARIANT 650
FT /note="V -> I (in dbSNP:rs2340601)"
FT /id="VAR_013695"
FT VARIANT 683
FT /note="S -> G (in dbSNP:rs3736689)"
FT /id="VAR_034101"
FT VARIANT 820
FT /note="Q -> R (in dbSNP:rs2272837)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_013696"
FT VARIANT 1179
FT /note="A -> E (in dbSNP:rs2272843)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_013697"
FT CONFLICT 321
FT /note="Q -> H (in Ref. 2; BAH13697)"
FT /evidence="ECO:0000305"
FT CONFLICT 1016
FT /note="L -> P (in Ref. 2; BAH13697)"
FT /evidence="ECO:0000305"
FT CONFLICT 1063
FT /note="I -> V (in Ref. 2; BAA90895)"
FT /evidence="ECO:0000305"
FT CONFLICT 1096
FT /note="F -> L (in Ref. 2; BAA90895)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1211 AA; 135293 MW; 410716BDCC85F8B1 CRC64;
MLSLAAKLVA FFWRTADTPR EEAGQLEPEL AEGDTKLKTV RGVVTRYCSD YGMIDDMIYF
SSDAVTSRVL LNVGQEVIAV VEENKVSNGL KAIRVEAVSD KWEDDSRNHG SPSDCGPRVL
IGCVTSLVEG AGCISQTTYF SLESVCEGFE PCKGDWVEAE YRIRPGTWSS EATSVKPLRY
KRVDKVCISS LCGRNGVLEE SIFFTLDSLK LPDGYTPRRG DVVNAVVVES SQSCYVWRAL
CMTLVKRRDA APVHEATHFY GTILLKNKGD IEVTQVTHFG TLKEGRSKTM VIWIENKGDI
PQNLVSCKLA GWDKSKQFRF QMLDKDQMCP VVSFVSVPEK ENSSDENINS LNSHTKNKTS
QMSESSLVNN RGISPGDCTC KGENGEKDNI LSRKQMTEPE PGGLVPPGGK TFIVVICDGK
NPGRCKELLL LCFSDFLIGR YLEVNVISGE ESLIAAREPF SWKKLKSSQA LTSAKTTVVV
TAQKRNSRRQ LPSFLPQYPI PDRLRKCVEQ KIDILTFQPL LAELLNMSNY KEKFSTLLWL
EEIYAEMELK EYNMSGIILR RNGDLLVLEV PGLAEGRPSL YAGDKLILKT QEYNGHAIEY
ISYVTEIHEE DVTLKINPEF EQAYNFEPMD VEFTYNRTTS RRCHFALEHV IHLGVKVLFP
EEIILQSPQV TGNWNHAQDT KSSGQSTSKK NRKTMTDQAE HGTEERRVGD KDLPVLAPFT
AEMSDWVDEI QTPKARKMEF FNPVLNENQK LAVKRILSGD CRPLPYILFG PPGTGKTVTI
IEAVLQVHFA LPDSRILVCA PSNSAADLVC LRLHESKVLQ PATMVRVNAT CRFEEIVIDA
VKPYCRDGED IWKASRFRII ITTCSSSGLF YQIGVRVGHF THVFVDEAGQ ASEPECLIPL
GLMSDISGQI VLAGDPMQLG PVIKSRLAMA YGLNVSFLER LMSRPAYQRD ENAFGACGAH
NPLLVTKLVK NYRSHEALLM LPSRLFYHRE LEVCADPTVV TSLLGWEKLP KKGFPLIFHG
VRGSEAREGK SPSWFNPAEA VQVLRYCCLL AHSISSQVSA SDIGVITPYR KQVEKIRILL
RNVDLMDIKV GSVEEFQGQE YLVIIISTVR SNEDRFEDDR YFLGFLSNSK RFNVAITRPK
ALLIVLGNPH VLVRDPCFGA LLEYSITNGV YMGCDLPPAL QSLQNCGEGV ADPSYPVVPE
STGPEKHQEP S
