ACD10_HUMAN
ID ACD10_HUMAN Reviewed; 1059 AA.
AC Q6JQN1; G3XAJ0; Q8N828; Q8NAP2; Q96BX5;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Acyl-CoA dehydrogenase family member 10;
DE Short=ACAD-10;
DE EC=1.3.99.-;
GN Name=ACAD10;
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=15560374; DOI=10.1023/b:mole.0000043622.57408.6b;
RA Ye X., Ji C., Zhou C., Zeng L., Gu S., Ying K., Xie Y., Mao Y.;
RT "Cloning and characterization of a human cDNA ACAD10 mapped to chromosome
RT 12q24.1.";
RL Mol. Biol. Rep. 31:191-195(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Brain, 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 5).
RC TISSUE=Bone marrow;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Skin;
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 [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=21237683; DOI=10.1016/j.ymgme.2010.12.005;
RA He M., Pei Z., Mohsen A.W., Watkins P., Murdoch G., Van Veldhoven P.P.,
RA Ensenauer R., Vockley J.;
RT "Identification and characterization of new long chain acyl-CoA
RT dehydrogenases.";
RL Mol. Genet. Metab. 102:418-429(2011).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Acyl-CoA dehydrogenase only active with R- and S-2-methyl-
CC C15-CoA. {ECO:0000269|PubMed:21237683}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + a 2,3-saturated acyl-CoA = a 2,3-dehydroacyl-CoA + AH2;
CC Xref=Rhea:RHEA:48608, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:60015, ChEBI:CHEBI:65111;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q6JQN1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6JQN1-2; Sequence=VSP_024634, VSP_024635;
CC Name=3;
CC IsoId=Q6JQN1-3; Sequence=VSP_024630, VSP_024633, VSP_024634,
CC VSP_024635;
CC Name=4;
CC IsoId=Q6JQN1-4; Sequence=VSP_024631, VSP_024632;
CC Name=5;
CC IsoId=Q6JQN1-5; Sequence=VSP_044980;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest expression in fetal
CC brain, followed by heart, muscle, kidney and adult brain. Expression
CC levels varying from isoform to isoform. {ECO:0000269|PubMed:15560374,
CC ECO:0000269|PubMed:21237683}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH15056.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY323912; AAQ88260.1; -; mRNA.
DR EMBL; AK092356; BAC03869.1; -; mRNA.
DR EMBL; AK097425; BAC05046.1; -; mRNA.
DR EMBL; AL832043; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC002996; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW97962.1; -; Genomic_DNA.
DR EMBL; BC015056; AAH15056.1; ALT_INIT; mRNA.
DR EMBL; BC126358; AAI26359.1; -; mRNA.
DR CCDS; CCDS31903.1; -. [Q6JQN1-1]
DR CCDS; CCDS44973.1; -. [Q6JQN1-5]
DR RefSeq; NP_001130010.1; NM_001136538.1. [Q6JQN1-5]
DR RefSeq; NP_079523.3; NM_025247.5. [Q6JQN1-1]
DR AlphaFoldDB; Q6JQN1; -.
DR SMR; Q6JQN1; -.
DR BioGRID; 123274; 124.
DR IntAct; Q6JQN1; 20.
DR STRING; 9606.ENSP00000389813; -.
DR ChEMBL; CHEMBL4105816; -.
DR GlyGen; Q6JQN1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6JQN1; -.
DR PhosphoSitePlus; Q6JQN1; -.
DR BioMuta; ACAD10; -.
DR DMDM; 74748862; -.
DR EPD; Q6JQN1; -.
DR jPOST; Q6JQN1; -.
DR MassIVE; Q6JQN1; -.
DR MaxQB; Q6JQN1; -.
DR PaxDb; Q6JQN1; -.
DR PeptideAtlas; Q6JQN1; -.
DR PRIDE; Q6JQN1; -.
DR ProteomicsDB; 33762; -.
DR ProteomicsDB; 66515; -. [Q6JQN1-1]
DR ProteomicsDB; 66516; -. [Q6JQN1-2]
DR ProteomicsDB; 66517; -. [Q6JQN1-3]
DR ProteomicsDB; 66518; -. [Q6JQN1-4]
DR Antibodypedia; 31114; 172 antibodies from 26 providers.
DR DNASU; 80724; -.
DR Ensembl; ENST00000313698.9; ENSP00000325137.5; ENSG00000111271.15. [Q6JQN1-1]
DR Ensembl; ENST00000455480.6; ENSP00000389813.2; ENSG00000111271.15. [Q6JQN1-5]
DR GeneID; 80724; -.
DR KEGG; hsa:80724; -.
DR MANE-Select; ENST00000313698.9; ENSP00000325137.5; NM_025247.6; NP_079523.3.
DR UCSC; uc001tsq.4; human. [Q6JQN1-1]
DR CTD; 80724; -.
DR DisGeNET; 80724; -.
DR GeneCards; ACAD10; -.
DR HGNC; HGNC:21597; ACAD10.
DR HPA; ENSG00000111271; Low tissue specificity.
DR MIM; 611181; gene.
DR neXtProt; NX_Q6JQN1; -.
DR OpenTargets; ENSG00000111271; -.
DR PharmGKB; PA134976754; -.
DR VEuPathDB; HostDB:ENSG00000111271; -.
DR eggNOG; KOG1469; Eukaryota.
DR eggNOG; KOG3085; Eukaryota.
DR GeneTree; ENSGT00940000161620; -.
DR HOGENOM; CLU_007526_2_1_1; -.
DR InParanoid; Q6JQN1; -.
DR OMA; PGIKVIR; -.
DR OrthoDB; 1028522at2759; -.
DR PhylomeDB; Q6JQN1; -.
DR TreeFam; TF333953; -.
DR PathwayCommons; Q6JQN1; -.
DR Reactome; R-HSA-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR SignaLink; Q6JQN1; -.
DR BioGRID-ORCS; 80724; 12 hits in 1086 CRISPR screens.
DR ChiTaRS; ACAD10; human.
DR GenomeRNAi; 80724; -.
DR Pharos; Q6JQN1; Tchem.
DR PRO; PR:Q6JQN1; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q6JQN1; protein.
DR Bgee; ENSG00000111271; Expressed in apex of heart and 192 other tissues.
DR ExpressionAtlas; Q6JQN1; baseline and differential.
DR Genevisible; Q6JQN1; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; NAS:UniProtKB.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0006635; P:fatty acid beta-oxidation; TAS:Reactome.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IBA:GO_Central.
DR CDD; cd05154; ACAD10_11_N-like; 1.
DR Gene3D; 1.10.150.240; -; 1.
DR Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR041726; ACAD10_11_N.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR InterPro; IPR002575; Aminoglycoside_PTrfase.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR011945; HAD-SF_ppase_IA/epoxid_hydro_N.
DR InterPro; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR Pfam; PF01636; APH; 1.
DR Pfam; PF13419; HAD_2; 1.
DR PRINTS; PR00413; HADHALOGNASE.
DR SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR02247; HAD-1A3-hyp; 1.
DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; FAD; Flavoprotein; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..1059
FT /note="Acyl-CoA dehydrogenase family member 10"
FT /id="PRO_0000284770"
FT BINDING 792..802
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 828
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 943
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 1013
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 1044
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT MOD_RES 413
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8K370"
FT MOD_RES 427
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8K370"
FT MOD_RES 427
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8K370"
FT MOD_RES 1052
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8K370"
FT MOD_RES 1052
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8K370"
FT VAR_SEQ 1..398
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_024630"
FT VAR_SEQ 230
FT /note="K -> KRQGFAVLPKLVSNSWAQAIYPPYPPKVVRLQ (in isoform
FT 5)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_044980"
FT VAR_SEQ 285
FT /note="P -> L (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024631"
FT VAR_SEQ 286..1059
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024632"
FT VAR_SEQ 399..413
FT /note="HSVDLQAVGLEDYGK -> MLEYLSLTFLISVKI (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_024633"
FT VAR_SEQ 883..890
FT /note="GHGEVRFE -> CFLPSFSL (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_024634"
FT VAR_SEQ 891..1059
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_024635"
FT VARIANT 200
FT /note="Q -> R (in dbSNP:rs35276160)"
FT /id="VAR_031811"
FT VARIANT 216
FT /note="T -> P (in dbSNP:rs35753710)"
FT /id="VAR_031812"
FT VARIANT 463
FT /note="D -> N (in dbSNP:rs36046440)"
FT /id="VAR_031813"
FT VARIANT 880
FT /note="A -> V (in dbSNP:rs34245489)"
FT /id="VAR_031814"
FT CONFLICT 124
FT /note="S -> P (in Ref. 2; BAC03869)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="C -> M (in Ref. 2; BAC05046)"
FT /evidence="ECO:0000305"
FT CONFLICT 511
FT /note="V -> M (in Ref. 3; AL832043)"
FT /evidence="ECO:0000305"
FT CONFLICT 641
FT /note="E -> D (in Ref. 3; AL832043)"
FT /evidence="ECO:0000305"
FT CONFLICT 663
FT /note="V -> D (in Ref. 2; BAC03869)"
FT /evidence="ECO:0000305"
FT CONFLICT 688
FT /note="H -> R (in Ref. 2; BAC03869)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1059 AA; 118834 MW; B8D4376FCF73D746 CRC64;
MCVRSCFQSP RLQWVWRTAF LKHTQRRHQG SHRWTHLGGS TYRAVIFDMG GVLIPSPGRV
AAEWEVQNRI PSGTILKALM EGGENGPWMR FMRAEITAEG FLREFGRLCS EMLKTSVPVD
SFFSLLTSER VAKQFPVMTE AITQIRAKGL QTAVLSNNFY LPNQKSFLPL DRKQFDVIVE
SCMEGICKPD PRIYKLCLEQ LGLQPSESIF LDDLGTNLKE AARLGIHTIK VNDPETAVKE
LEALLGFTLR VGVPNTRPVK KTMEIPKDSL QKYLKDLLGI QTTGPLELLQ FDHGQSNPTY
YIRLANRDLV LRKKPPGTLL PSAHAIEREF RIMKALANAG VPVPNVLDLC EDSSVIGTPF
YVMEYCPGLI YKDPSLPGLE PSHRRAIYTA MNTVLCKIHS VDLQAVGLED YGKQGDYIPR
QVRTWVKQYR ASETSTIPAM ERLIEWLPLH LPRQQRTTVV HGDFRLDNLV FHPEEPEVLA
VLDWELSTLG DPLADVAYSC LAHYLPSSFP VLRGINDCDL TQLGIPAAEE YFRMYCLQMG
LPPTENWNFY MAFSFFRVAA ILQGVYKRSL TGQASSTYAE QTGKLTEFVS NLAWDFAVKE
GFRVFKEMPF TNPLTRSYHT WARPQSQWCP TGSRSYSSVP EASPAHTSRG GLVISPESLS
PPVRELYHRL KHFMEQRVYP AEPELQSHQA SAARWSPSPL IEDLKEKAKA EGLWNLFLPL
EADPEKKYGA GLTNVEYAHL CELMGTSLYA PEVCNCSAPD TGNMELLVRY GTEAQKARWL
IPLLEGKARS CFAMTEPQVA SSDATNIEAS IREEDSFYVI NGHKWWITGI LDPRCQLCVF
MGKTDPHAPR HRQQSVLLVP MDTPGIKIIR PLTVYGLEDA PGGHGEVRFE HVRVPKENMV
LGPGRGFEIA QGRLGPGRIH HCMRLIGFSE RALALMKARV KSRLAFGKPL VEQGTVLADI
AQSRVEIEQA RLLVLRAAHL MDLAGNKAAA LDIAMIKMVA PSMASRVIDR AIQAFGAAGL
SSDYPLAQFF TWARALRFAD GPDEVHRATV AKLELKHRI
