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   27-MAR-2024, entry version 163.
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; 136.
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   SwissPalm; Q6JQN1; -.
DR   BioMuta; ACAD10; -.
DR   DMDM; 74748862; -.
DR   EPD; Q6JQN1; -.
DR   jPOST; Q6JQN1; -.
DR   MassIVE; Q6JQN1; -.
DR   MaxQB; Q6JQN1; -.
DR   PaxDb; 9606-ENSP00000389813; -.
DR   PeptideAtlas; 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   Pumba; Q6JQN1; -.
DR   Antibodypedia; 31114; 185 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   AGR; HGNC:21597; -.
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; KNWNFYM; -.
DR   OrthoDB; 276350at2759; -.
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; 16 hits in 1166 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 194 other cell types or tissues.
DR   ExpressionAtlas; Q6JQN1; baseline and differential.
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   CDD; cd02603; HAD_sEH-N_like; 1.
DR   Gene3D; 3.90.1200.10; -; 1.
DR   Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR   Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR   Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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_sf.
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; IPR023214; HAD_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR023198; PGP-like_dom2.
DR   NCBIfam; TIGR02247; HAD-1A3-hyp; 1.
DR   NCBIfam; TIGR01509; HAD-SF-IA-v3; 1.
DR   PANTHER; PTHR47829:SF1; AMINOGLYCOSIDE PHOSPHOTRANSFERASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR47829; HYDROLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G12880)-RELATED; 1.
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; PF00702; Hydrolase; 1.
DR   PRINTS; PR00413; HADHALOGNASE.
DR   SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   Genevisible; Q6JQN1; HS.
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
//