TIDC1_HUMAN
ID TIDC1_HUMAN Reviewed; 285 AA.
AC Q9NPL8; D3DN81; Q6IAJ7; Q6UWU6; Q9NPR3; Q9NPS5; Q9P0Y6;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Complex I assembly factor TIMMDC1, mitochondrial {ECO:0000305};
DE AltName: Full=Protein M5-14;
DE AltName: Full=Translocase of inner mitochondrial membrane domain-containing protein 1;
DE Short=TIMM domain containing-protein 1;
GN Name=TIMMDC1 {ECO:0000312|HGNC:HGNC:1321}; Synonyms=C3orf1;
GN ORFNames=UNQ247/PRO284;
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], VARIANTS ASP-76 AND ILE-217, AND TISSUE
RP SPECIFICITY.
RX PubMed=11092749; DOI=10.3109/10425170009033252;
RA Escarceller M., Pluvinet R., Sumoy L., Estivill X.;
RT "Identification and expression analysis of C3orf1, a novel human gene
RT homologous to the Drosophila RP140-upstream gene.";
RL DNA Seq. 11:335-338(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Li D.X., Roberts R.;
RT "Identification of a novel transcript, M5-14, preferentially expressed in
RT cardiac and skeletal muscle.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-217.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=B-cell;
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 [8]
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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=24191001; DOI=10.1073/pnas.1319247110;
RA Andrews B., Carroll J., Ding S., Fearnley I.M., Walker J.E.;
RT "Assembly factors for the membrane arm of human complex I.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:18934-18939(2013).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277, AND IDENTIFICATION BY
RP 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).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [12]
RP INTERACTION WITH TMEM70.
RX PubMed=33753518; DOI=10.1073/pnas.2100558118;
RA Carroll J., He J., Ding S., Fearnley I.M., Walker J.E.;
RT "TMEM70 and TMEM242 help to assemble the rotor ring of human ATP synthase
RT and interact with assembly factors for complex I.";
RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021).
RN [13]
RP INVOLVEMENT IN MC1DN31.
RX PubMed=28604674; DOI=10.1038/ncomms15824;
RA Kremer L.S., Bader D.M., Mertes C., Kopajtich R., Pichler G., Iuso A.,
RA Haack T.B., Graf E., Schwarzmayr T., Terrile C., Konarikova E., Repp B.,
RA Kastenmueller G., Adamski J., Lichtner P., Leonhardt C., Funalot B.,
RA Donati A., Tiranti V., Lombes A., Jardel C., Glaeser D., Taylor R.W.,
RA Ghezzi D., Mayr J.A., Roetig A., Freisinger P., Distelmaier F., Strom T.M.,
RA Meitinger T., Gagneur J., Prokisch H.;
RT "Genetic diagnosis of Mendelian disorders via RNA sequencing.";
RL Nat. Commun. 8:15824-15824(2017).
CC -!- FUNCTION: Chaperone protein involved in the assembly of the
CC mitochondrial NADH:ubiquinone oxidoreductase complex (complex I).
CC Participates in constructing the membrane arm of complex I.
CC {ECO:0000269|PubMed:24191001}.
CC -!- SUBUNIT: Associates with the intermediate 315 kDa subcomplex of
CC incompletely assembled complex I. Interacts with TMEM70
CC (PubMed:33753518). {ECO:0000269|PubMed:24191001,
CC ECO:0000269|PubMed:33753518}.
CC -!- INTERACTION:
CC Q9NPL8; Q8TD06: AGR3; NbExp=3; IntAct=EBI-6268651, EBI-3925742;
CC Q9NPL8; Q86W74-2: ANKRD46; NbExp=3; IntAct=EBI-6268651, EBI-12109402;
CC Q9NPL8; P55056: APOC4; NbExp=3; IntAct=EBI-6268651, EBI-18302142;
CC Q9NPL8; O95236-2: APOL3; NbExp=3; IntAct=EBI-6268651, EBI-11976321;
CC Q9NPL8; Q8N6S5: ARL6IP6; NbExp=3; IntAct=EBI-6268651, EBI-2808844;
CC Q9NPL8; O75787: ATP6AP2; NbExp=3; IntAct=EBI-6268651, EBI-2512037;
CC Q9NPL8; P51572: BCAP31; NbExp=3; IntAct=EBI-6268651, EBI-77683;
CC Q9NPL8; Q8WVX3-2: C4orf3; NbExp=3; IntAct=EBI-6268651, EBI-12003442;
CC Q9NPL8; Q6UWT4: C5orf46; NbExp=3; IntAct=EBI-6268651, EBI-11986083;
CC Q9NPL8; P13236: CCL4; NbExp=3; IntAct=EBI-6268651, EBI-2873970;
CC Q9NPL8; O95674: CDS2; NbExp=3; IntAct=EBI-6268651, EBI-3913685;
CC Q9NPL8; Q8TAZ6: CMTM2; NbExp=3; IntAct=EBI-6268651, EBI-2339374;
CC Q9NPL8; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-6268651, EBI-6942903;
CC Q9NPL8; Q9HCS2: CYP4F12; NbExp=3; IntAct=EBI-6268651, EBI-3918831;
CC Q9NPL8; Q96PD2-2: DCBLD2; NbExp=3; IntAct=EBI-6268651, EBI-12135455;
CC Q9NPL8; Q9NR28: DIABLO; NbExp=3; IntAct=EBI-6268651, EBI-517508;
CC Q9NPL8; Q8N682: DRAM1; NbExp=3; IntAct=EBI-6268651, EBI-10305400;
CC Q9NPL8; Q6UW88-2: EPGN; NbExp=3; IntAct=EBI-6268651, EBI-17468158;
CC Q9NPL8; O75063: FAM20B; NbExp=3; IntAct=EBI-6268651, EBI-11090967;
CC Q9NPL8; Q96KR6: FAM210B; NbExp=3; IntAct=EBI-6268651, EBI-18938272;
CC Q9NPL8; Q969F0: FATE1; NbExp=4; IntAct=EBI-6268651, EBI-743099;
CC Q9NPL8; Q14802-3: FXYD3; NbExp=3; IntAct=EBI-6268651, EBI-12175685;
CC Q9NPL8; P29033: GJB2; NbExp=3; IntAct=EBI-6268651, EBI-3905204;
CC Q9NPL8; Q8TDV0: GPR151; NbExp=3; IntAct=EBI-6268651, EBI-11955647;
CC Q9NPL8; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-6268651, EBI-13345167;
CC Q9NPL8; Q8TED1: GPX8; NbExp=3; IntAct=EBI-6268651, EBI-11721746;
CC Q9NPL8; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-6268651, EBI-18053395;
CC Q9NPL8; P01563: IFNA2; NbExp=3; IntAct=EBI-6268651, EBI-4394394;
CC Q9NPL8; Q99706: KIR2DL4; NbExp=3; IntAct=EBI-6268651, EBI-10294579;
CC Q9NPL8; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-6268651, EBI-2820517;
CC Q9NPL8; Q9NX47: MARCHF5; NbExp=3; IntAct=EBI-6268651, EBI-2341610;
CC Q9NPL8; Q5SR56: MFSD14B; NbExp=3; IntAct=EBI-6268651, EBI-373355;
CC Q9NPL8; Q6N075: MFSD5; NbExp=3; IntAct=EBI-6268651, EBI-3920969;
CC Q9NPL8; Q9NX14: NDUFB11; NbExp=3; IntAct=EBI-6268651, EBI-1246182;
CC Q9NPL8; Q92982: NINJ1; NbExp=3; IntAct=EBI-6268651, EBI-2802124;
CC Q9NPL8; Q8N912: NRAC; NbExp=3; IntAct=EBI-6268651, EBI-12051377;
CC Q9NPL8; P50542-3: PEX5; NbExp=3; IntAct=EBI-6268651, EBI-12181987;
CC Q9NPL8; Q07326: PIGF; NbExp=3; IntAct=EBI-6268651, EBI-17180304;
CC Q9NPL8; P18031: PTPN1; NbExp=3; IntAct=EBI-6268651, EBI-968788;
CC Q9NPL8; Q16849-3: PTPRN; NbExp=3; IntAct=EBI-6268651, EBI-10200782;
CC Q9NPL8; Q9Y225-2: RNF24; NbExp=3; IntAct=EBI-6268651, EBI-13044680;
CC Q9NPL8; Q8TAC9: SCAMP5; NbExp=3; IntAct=EBI-6268651, EBI-2695784;
CC Q9NPL8; O00767: SCD; NbExp=3; IntAct=EBI-6268651, EBI-2684237;
CC Q9NPL8; O75920: SERF1B; NbExp=3; IntAct=EBI-6268651, EBI-2115181;
CC Q9NPL8; Q8N6R1: SERP2; NbExp=3; IntAct=EBI-6268651, EBI-749270;
CC Q9NPL8; Q6ICL7: SLC35E4; NbExp=3; IntAct=EBI-6268651, EBI-12867720;
CC Q9NPL8; Q8N357: SLC35F6; NbExp=3; IntAct=EBI-6268651, EBI-713484;
CC Q9NPL8; Q96JF0-2: ST6GAL2; NbExp=3; IntAct=EBI-6268651, EBI-12908338;
CC Q9NPL8; Q86Y82: STX12; NbExp=3; IntAct=EBI-6268651, EBI-2691717;
CC Q9NPL8; O43752: STX6; NbExp=3; IntAct=EBI-6268651, EBI-2695795;
CC Q9NPL8; Q7Z5S9: TMEM144; NbExp=3; IntAct=EBI-6268651, EBI-12876358;
CC Q9NPL8; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-6268651, EBI-8638294;
CC Q9NPL8; Q96HP8: TMEM176A; NbExp=3; IntAct=EBI-6268651, EBI-2800645;
CC Q9NPL8; Q8N511: TMEM199; NbExp=3; IntAct=EBI-6268651, EBI-10265825;
CC Q9NPL8; Q969S6: TMEM203; NbExp=3; IntAct=EBI-6268651, EBI-12274070;
CC Q9NPL8; Q8WW34-2: TMEM239; NbExp=3; IntAct=EBI-6268651, EBI-11528917;
CC Q9NPL8; Q969K7: TMEM54; NbExp=3; IntAct=EBI-6268651, EBI-3922833;
CC Q9NPL8; Q6PI78: TMEM65; NbExp=3; IntAct=EBI-6268651, EBI-6656213;
CC Q9NPL8; Q8N2M4: TMEM86A; NbExp=3; IntAct=EBI-6268651, EBI-12015604;
CC Q9NPL8; Q5BVD1: TTMP; NbExp=3; IntAct=EBI-6268651, EBI-10243654;
CC Q9NPL8; Q9NYZ1: TVP23B; NbExp=3; IntAct=EBI-6268651, EBI-11343401;
CC Q9NPL8; Q86WB7-2: UNC93A; NbExp=3; IntAct=EBI-6268651, EBI-13356252;
CC Q9NPL8; O95070: YIF1A; NbExp=3; IntAct=EBI-6268651, EBI-2799703;
CC Q9NPL8; Q9Y548: YIPF1; NbExp=3; IntAct=EBI-6268651, EBI-7850136;
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000269|PubMed:24191001}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:24191001}.
CC -!- TISSUE SPECIFICITY: Generalized expression enhanced in heart and
CC skeletal muscle. {ECO:0000269|PubMed:11092749}.
CC -!- DISEASE: Mitochondrial complex I deficiency, nuclear type 31 (MC1DN31)
CC [MIM:618251]: A form of mitochondrial complex I deficiency, the most
CC common biochemical signature of mitochondrial disorders, a group of
CC highly heterogeneous conditions characterized by defective oxidative
CC phosphorylation, which collectively affects 1 in 5-10000 live births.
CC Clinical disorders have variable severity, ranging from lethal neonatal
CC disease to adult-onset neurodegenerative disorders. Phenotypes include
CC macrocephaly with progressive leukodystrophy, non-specific
CC encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh
CC syndrome, Leber hereditary optic neuropathy, and some forms of
CC Parkinson disease. MC1DN31 transmission pattern is consistent with
CC autosomal recessive inheritance. {ECO:0000269|PubMed:28604674}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the Tim17/Tim22/Tim23 family. {ECO:0000305}.
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DR EMBL; AF210057; AAG43510.1; -; mRNA.
DR EMBL; AL390077; CAB98201.1; -; mRNA.
DR EMBL; AL390090; CAB98212.1; -; mRNA.
DR EMBL; AL390094; CAB98251.1; -; mRNA.
DR EMBL; AF139077; AAF62372.1; -; mRNA.
DR EMBL; AL136622; CAB66557.1; -; mRNA.
DR EMBL; AY358633; AAQ88996.1; -; mRNA.
DR EMBL; CR457158; CAG33439.1; -; mRNA.
DR EMBL; CR533524; CAG38555.1; -; mRNA.
DR EMBL; CH471052; EAW79566.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79568.1; -; Genomic_DNA.
DR EMBL; BC012341; AAH12341.1; -; mRNA.
DR CCDS; CCDS33831.1; -.
DR RefSeq; NP_057673.2; NM_016589.3.
DR AlphaFoldDB; Q9NPL8; -.
DR BioGRID; 119451; 241.
DR IntAct; Q9NPL8; 130.
DR MINT; Q9NPL8; -.
DR STRING; 9606.ENSP00000418803; -.
DR iPTMnet; Q9NPL8; -.
DR PhosphoSitePlus; Q9NPL8; -.
DR SwissPalm; Q9NPL8; -.
DR BioMuta; TIMMDC1; -.
DR DMDM; 116243026; -.
DR EPD; Q9NPL8; -.
DR jPOST; Q9NPL8; -.
DR MassIVE; Q9NPL8; -.
DR MaxQB; Q9NPL8; -.
DR PaxDb; Q9NPL8; -.
DR PeptideAtlas; Q9NPL8; -.
DR PRIDE; Q9NPL8; -.
DR ProteomicsDB; 82035; -.
DR Antibodypedia; 53806; 39 antibodies from 15 providers.
DR DNASU; 51300; -.
DR Ensembl; ENST00000494664.6; ENSP00000418803.1; ENSG00000113845.10.
DR GeneID; 51300; -.
DR KEGG; hsa:51300; -.
DR MANE-Select; ENST00000494664.6; ENSP00000418803.1; NM_016589.4; NP_057673.2.
DR UCSC; uc003ecn.4; human.
DR CTD; 51300; -.
DR DisGeNET; 51300; -.
DR GeneCards; TIMMDC1; -.
DR HGNC; HGNC:1321; TIMMDC1.
DR HPA; ENSG00000113845; Low tissue specificity.
DR MalaCards; TIMMDC1; -.
DR MIM; 615534; gene.
DR MIM; 618251; phenotype.
DR neXtProt; NX_Q9NPL8; -.
DR OpenTargets; ENSG00000113845; -.
DR Orphanet; 2609; Isolated complex I deficiency.
DR PharmGKB; PA25900; -.
DR VEuPathDB; HostDB:ENSG00000113845; -.
DR eggNOG; KOG4608; Eukaryota.
DR GeneTree; ENSGT00390000013817; -.
DR HOGENOM; CLU_068982_0_0_1; -.
DR InParanoid; Q9NPL8; -.
DR OMA; WQYKWRL; -.
DR OrthoDB; 1366254at2759; -.
DR PhylomeDB; Q9NPL8; -.
DR TreeFam; TF324676; -.
DR PathwayCommons; Q9NPL8; -.
DR Reactome; R-HSA-6799198; Complex I biogenesis.
DR SignaLink; Q9NPL8; -.
DR BioGRID-ORCS; 51300; 169 hits in 1089 CRISPR screens.
DR ChiTaRS; TIMMDC1; human.
DR GeneWiki; C3orf1; -.
DR GenomeRNAi; 51300; -.
DR Pharos; Q9NPL8; Tbio.
DR PRO; PR:Q9NPL8; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9NPL8; protein.
DR Bgee; ENSG00000113845; Expressed in left ventricle myocardium and 185 other tissues.
DR ExpressionAtlas; Q9NPL8; baseline and differential.
DR Genevisible; Q9NPL8; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:LIFEdb.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
PE 1: Evidence at protein level;
KW Chaperone; Membrane; Mitochondrion; Phosphoprotein;
KW Primary mitochondrial disease; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..285
FT /note="Complex I assembly factor TIMMDC1, mitochondrial"
FT /id="PRO_0000252478"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VARIANT 76
FT /note="N -> D (in dbSNP:rs11539377)"
FT /evidence="ECO:0000269|PubMed:11092749"
FT /id="VAR_027885"
FT VARIANT 217
FT /note="V -> I (in dbSNP:rs57168946)"
FT /evidence="ECO:0000269|PubMed:11092749, ECO:0000269|Ref.5"
FT /id="VAR_061572"
FT CONFLICT 156
FT /note="L -> P (in Ref. 5; CAG33439)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="S -> A (in Ref. 4; AAQ88996)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="Q -> R (in Ref. 4; AAQ88996)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 285 AA; 32178 MW; 5AA6474C3ABCCFA2 CRC64;
MEVPPPAPRS FLCRALCLFP RVFAAEAVTA DSEVLEERQK RLPYVPEPYY PESGWDRLRE
LFGKDEQQRI SKDLANICKT AATAGIIGWV YGGIPAFIHA KQQYIEQSQA EIYHNRFDAV
QSAHRAATRG FIRYGWRWGW RTAVFVTIFN TVNTSLNVYR NKDALSHFVI AGAVTGSLFR
INVGLRGLVA GGIIGALLGT PVGGLLMAFQ KYSGETVQER KQKDRKALHE LKLEEWKGRL
QVTEHLPEKI ESSLQEDEPE NDAKKIEALL NLPRNPSVID KQDKD
