ID   COA6_HUMAN              Reviewed;         125 AA.
AC   Q5JTJ3; Q5JTJ2; Q5JTJ4; Q8TA88;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   24-JAN-2024, entry version 146.
DE   RecName: Full=Cytochrome c oxidase assembly factor 6 homolog;
GN   Name=COA6; Synonyms=C1orf31;
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 [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Ovary, and Testis;
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   [3]
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   [4]
RP   INTERACTION WITH COA1.
RX   PubMed=22356826; DOI=10.1186/gb-2012-13-2-r12;
RA   Szklarczyk R., Wanschers B.F., Cuypers T.D., Esseling J.J., Riemersma M.,
RA   van den Brand M.A., Gloerich J., Lasonder E., van den Heuvel L.P.,
RA   Nijtmans L.G., Huynen M.A.;
RT   "Iterative orthology prediction uncovers new mitochondrial proteins and
RT   identifies C12orf62 as the human ortholog of COX14, a protein involved in
RT   the assembly of cytochrome c oxidase.";
RL   Genome Biol. 13:RESEARCH0012.1-RESEARCH0012.14(2012).
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM 3), CLEAVAGE OF
RP   INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 3), AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [6]
RP   FUNCTION, INVOLVEMENT IN MC4DN13, AND VARIANT MC4DN13 CYS-59.
RX   PubMed=24549041; DOI=10.1093/hmg/ddu069;
RA   Ghosh A., Trivedi P.P., Timbalia S.A., Griffin A.T., Rahn J.J., Chan S.S.,
RA   Gohil V.M.;
RT   "Copper supplementation restores cytochrome c oxidase assembly defect in a
RT   mitochondrial disease model of COA6 deficiency.";
RL   Hum. Mol. Genet. 23:3596-3606(2014).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MT-CO2 AND SCO2, AND
RP   CHARACTERIZATION OF VARIANT MC4DN13 CYS-59.
RX   PubMed=25959673; DOI=10.1016/j.cmet.2015.04.012;
RA   Pacheu-Grau D., Bareth B., Dudek J., Juris L., Voegtle F.N., Wissel M.,
RA   Leary S.C., Dennerlein S., Rehling P., Deckers M.;
RT   "Cooperation between COA6 and SCO2 in COX2 maturation during cytochrome c
RT   oxidase assembly links two mitochondrial cardiomyopathies.";
RL   Cell Metab. 21:823-833(2015).
RN   [8]
RP   FUNCTION, AND INTERACTION WITH SCO1.
RX   PubMed=26160915; DOI=10.1093/hmg/ddv265;
RA   Stroud D.A., Maher M.J., Lindau C., Voegtle F.N., Frazier A.E.,
RA   Surgenor E., Mountford H., Singh A.P., Bonas M., Oeljeklaus S.,
RA   Warscheid B., Meisinger C., Thorburn D.R., Ryan M.T.;
RT   "COA6 is a mitochondrial complex IV assembly factor critical for biogenesis
RT   of mtDNA-encoded COX2.";
RL   Hum. Mol. Genet. 24:5404-5415(2015).
RN   [9]
RP   SUBCELLULAR LOCATION, INVOLVEMENT IN MC4DN13, AND VARIANT MC4DN13 ARG-66.
RX   PubMed=25339201; DOI=10.1002/humu.22715;
RA   Baertling F., van den Brand M.A.M., Hertecant J.L., Al-Shamsi A.,
RA   van den Heuvel L.P., Distelmaier F., Mayatepek E., Smeitink J.A.,
RA   Nijtmans L.G., Rodenburg R.J.;
RT   "Mutations in COA6 cause cytochrome c oxidase deficiency and neonatal
RT   hypertrophic cardiomyopathy.";
RL   Hum. Mutat. 36:34-38(2015).
RN   [10]
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   [11]
RP   IDENTIFICATION IN A COMPLEX WITH TMEM177; MT-CO2; COX20; COX18; SCO1 AND
RP   SCO2, AND INTERACTION WITH COX20.
RX   PubMed=29154948; DOI=10.1016/j.bbamcr.2017.11.010;
RA   Lorenzi I., Oeljeklaus S., Aich A., Ronsoer C., Callegari S., Dudek J.,
RA   Warscheid B., Dennerlein S., Rehling P.;
RT   "The mitochondrial TMEM177 associates with COX20 during COX2 biogenesis.";
RL   Biochim. Biophys. Acta 1865:323-333(2017).
RN   [12]
RP   INTERACTION WITH COX20.
RX   PubMed=28330871; DOI=10.1074/jbc.m117.778514;
RA   Bourens M., Barrientos A.;
RT   "Human mitochondrial cytochrome c oxidase assembly factor COX18 acts
RT   transiently as a membrane insertase within the subunit 2 maturation
RT   module.";
RL   J. Biol. Chem. 292:7774-7783(2017).
RN   [13]
RP   INTERACTION WITH COX16.
RX   PubMed=29381136; DOI=10.7554/elife.32572;
RA   Aich A., Wang C., Chowdhury A., Ronsoer C., Pacheu-Grau D.,
RA   Richter-Dennerlein R., Dennerlein S., Rehling P.;
RT   "COX16 promotes COX2 metallation and assembly during respiratory complex IV
RT   biogenesis.";
RL   Elife 7:0-0(2018).
CC   -!- FUNCTION: Involved in the maturation of the mitochondrial respiratory
CC       chain complex IV subunit MT-CO2/COX2. Thereby, may regulate early steps
CC       of complex IV assembly. Mitochondrial respiratory chain complex IV or
CC       cytochrome c oxidase is the component of the respiratory chain that
CC       catalyzes the transfer of electrons from intermembrane space cytochrome
CC       c to molecular oxygen in the matrix and as a consequence contributes to
CC       the proton gradient involved in mitochondrial ATP synthesis. May also
CC       be required for efficient formation of respiratory supercomplexes
CC       comprised of complexes III and IV. {ECO:0000269|PubMed:24549041,
CC       ECO:0000269|PubMed:25959673, ECO:0000269|PubMed:26160915}.
CC   -!- SUBUNIT: Interacts with COA1 (PubMed:22356826). Found in a complex with
CC       TMEM177, COX20, MT-CO2/COX2, COX18, SCO1 and SCO2 (PubMed:29154948).
CC       Interacts with MT-CO2/COX2 and SCO2 (PubMed:25959673). Interacts with
CC       SCO1 (PubMed:26160915). Interacts with COX20 in a MT-CO2/COX2- and
CC       COX18-dependent manner (PubMed:29154948, PubMed:28330871). Interacts
CC       with COX16 (PubMed:29381136). {ECO:0000269|PubMed:22356826,
CC       ECO:0000269|PubMed:25959673, ECO:0000269|PubMed:26160915,
CC       ECO:0000269|PubMed:29154948, ECO:0000269|PubMed:29381136}.
CC   -!- INTERACTION:
CC       Q5JTJ3; Q9NPB3: CABP2; NbExp=3; IntAct=EBI-2874677, EBI-12011224;
CC       Q5JTJ3; Q86UW9: DTX2; NbExp=3; IntAct=EBI-2874677, EBI-740376;
CC       Q5JTJ3; Q6DKK2: TTC19; NbExp=3; IntAct=EBI-2874677, EBI-948354;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC       {ECO:0000269|PubMed:25339201, ECO:0000269|PubMed:25959673}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q5JTJ3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5JTJ3-2; Sequence=VSP_023656;
CC       Name=3;
CC         IsoId=Q5JTJ3-3; Sequence=VSP_023655;
CC   -!- DISEASE: Mitochondrial complex IV deficiency, nuclear type 13 (MC4DN13)
CC       [MIM:616501]: An autosomal recessive, infantile disorder with a fatal
CC       course in the first weeks of life, characterized by hypertrophic
CC       cardiomyopathy, left ventricular non-compaction, lactic acidosis,
CC       metabolic hypotonia, and mitochondrial complex IV deficiency.
CC       {ECO:0000269|PubMed:24549041, ECO:0000269|PubMed:25339201,
CC       ECO:0000269|PubMed:25959673}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 6B family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH25793.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAH25793.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=LOVD-Leiden Open Variation Database; Note=cytochrome
CC       c oxidase assembly factor 6 homolog (S.cerevisiae) (COA6);
CC       URL="https://databases.lovd.nl/shared/genes/COA6";
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DR   EMBL; AL355472; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC025793; AAH25793.1; ALT_SEQ; mRNA.
DR   EMBL; BC116455; AAI16456.1; -; mRNA.
DR   CCDS; CCDS31059.1; -. [Q5JTJ3-1]
DR   CCDS; CCDS55690.1; -. [Q5JTJ3-3]
DR   CCDS; CCDS76275.1; -. [Q5JTJ3-2]
DR   RefSeq; NP_001013003.1; NM_001012985.2. [Q5JTJ3-1]
DR   RefSeq; NP_001193570.2; NM_001206641.2. [Q5JTJ3-2]
DR   RefSeq; NP_001288662.1; NM_001301733.1. [Q5JTJ3-3]
DR   PDB; 6NL3; NMR; -; A=47-125.
DR   PDB; 6PCE; X-ray; 1.65 A; A/B=50-119.
DR   PDB; 6PCF; X-ray; 2.20 A; A/B/C/D=49-113.
DR   PDBsum; 6NL3; -.
DR   PDBsum; 6PCE; -.
DR   PDBsum; 6PCF; -.
DR   AlphaFoldDB; Q5JTJ3; -.
DR   SMR; Q5JTJ3; -.
DR   BioGRID; 132839; 29.
DR   IntAct; Q5JTJ3; 14.
DR   STRING; 9606.ENSP00000355574; -.
DR   GlyGen; Q5JTJ3; 3 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; Q5JTJ3; -.
DR   PhosphoSitePlus; Q5JTJ3; -.
DR   BioMuta; COA6; -.
DR   DMDM; 74742178; -.
DR   EPD; Q5JTJ3; -.
DR   jPOST; Q5JTJ3; -.
DR   MassIVE; Q5JTJ3; -.
DR   MaxQB; Q5JTJ3; -.
DR   PaxDb; 9606-ENSP00000355572; -.
DR   PeptideAtlas; Q5JTJ3; -.
DR   ProteomicsDB; 63221; -. [Q5JTJ3-1]
DR   ProteomicsDB; 63222; -. [Q5JTJ3-2]
DR   ProteomicsDB; 63223; -. [Q5JTJ3-3]
DR   Pumba; Q5JTJ3; -.
DR   Antibodypedia; 34692; 115 antibodies from 20 providers.
DR   DNASU; 388753; -.
DR   Ensembl; ENST00000366612.1; ENSP00000355571.1; ENSG00000168275.16. [Q5JTJ3-3]
DR   Ensembl; ENST00000366613.1; ENSP00000355572.1; ENSG00000168275.16. [Q5JTJ3-1]
DR   Ensembl; ENST00000366615.10; ENSP00000355574.5; ENSG00000168275.16. [Q5JTJ3-2]
DR   Ensembl; ENST00000619305.1; ENSP00000479686.1; ENSG00000168275.16. [Q5JTJ3-3]
DR   GeneID; 388753; -.
DR   KEGG; hsa:388753; -.
DR   MANE-Select; ENST00000366615.10; ENSP00000355574.5; NM_001206641.3; NP_001193570.2. [Q5JTJ3-2]
DR   UCSC; uc001hwc.4; human. [Q5JTJ3-1]
DR   AGR; HGNC:18025; -.
DR   CTD; 388753; -.
DR   DisGeNET; 388753; -.
DR   GeneCards; COA6; -.
DR   HGNC; HGNC:18025; COA6.
DR   HPA; ENSG00000168275; Low tissue specificity.
DR   MalaCards; COA6; -.
DR   MIM; 614772; gene.
DR   MIM; 616501; phenotype.
DR   neXtProt; NX_Q5JTJ3; -.
DR   OpenTargets; ENSG00000168275; -.
DR   Orphanet; 1561; Fatal infantile cytochrome C oxidase deficiency.
DR   PharmGKB; PA25617; -.
DR   VEuPathDB; HostDB:ENSG00000168275; -.
DR   eggNOG; KOG3057; Eukaryota.
DR   GeneTree; ENSGT00390000004094; -.
DR   HOGENOM; CLU_142408_4_0_1; -.
DR   InParanoid; Q5JTJ3; -.
DR   OMA; RDEYWRC; -.
DR   OrthoDB; 7697at2759; -.
DR   PhylomeDB; Q5JTJ3; -.
DR   TreeFam; TF335992; -.
DR   PathwayCommons; Q5JTJ3; -.
DR   Reactome; R-HSA-1268020; Mitochondrial protein import.
DR   SignaLink; Q5JTJ3; -.
DR   BioGRID-ORCS; 388753; 207 hits in 1162 CRISPR screens.
DR   ChiTaRS; COA6; human.
DR   GenomeRNAi; 388753; -.
DR   Pharos; Q5JTJ3; Tbio.
DR   PRO; PR:Q5JTJ3; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q5JTJ3; Protein.
DR   Bgee; ENSG00000168275; Expressed in left ventricle myocardium and 180 other cell types or tissues.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IEA:GOC.
DR   GO; GO:0045277; C:respiratory chain complex IV; IEA:InterPro.
DR   GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0042775; P:mitochondrial ATP synthesis coupled electron transport; IMP:UniProtKB.
DR   GO; GO:0042774; P:plasma membrane ATP synthesis coupled electron transport; IMP:UniProtKB.
DR   GO; GO:0008535; P:respiratory chain complex IV assembly; IDA:UniProtKB.
DR   CDD; cd00926; Cyt_c_Oxidase_VIb; 1.
DR   Gene3D; 1.10.10.140; Cytochrome c oxidase, subunit VIb; 1.
DR   InterPro; IPR042289; COA6.
DR   InterPro; IPR048280; COX6B-like.
DR   InterPro; IPR003213; Cyt_c_oxidase_su6B.
DR   InterPro; IPR036549; Cyt_c_oxidase_su6B_sf.
DR   PANTHER; PTHR46690; CYTOCHROME C OXIDASE ASSEMBLY FACTOR 6 HOMOLOG; 1.
DR   PANTHER; PTHR46690:SF1; CYTOCHROME C OXIDASE ASSEMBLY FACTOR 6 HOMOLOG; 1.
DR   Pfam; PF02297; COX6B; 1.
DR   SUPFAM; SSF47694; Cytochrome c oxidase subunit h; 1.
DR   PROSITE; PS51808; CHCH; 1.
DR   Genevisible; Q5JTJ3; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Disease variant;
KW   Disulfide bond; Mitochondrion; Primary mitochondrial disease;
KW   Reference proteome.
FT   CHAIN           1..125
FT                   /note="Cytochrome c oxidase assembly factor 6 homolog"
FT                   /id="PRO_0000280399"
FT   DOMAIN          55..98
FT                   /note="CHCH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOTIF           58..68
FT                   /note="Cx9C motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOTIF           79..90
FT                   /note="Cx10C motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   DISULFID        58..90
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   DISULFID        68..79
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   VAR_SEQ         1..46
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_023655"
FT   VAR_SEQ         1..40
FT                   /note="MGPGGPLLSPSRGFLLCKTGWHSNRLLGDCGPHTPVSTAL -> MVARKGQK
FT                   SPRFRRVSCFLRLGRSTLLELEPAGRPCSGRTRHRALHRRLVACVTVSSRRHRKEAGRG
FT                   RAE (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_023656"
FT   VARIANT         59
FT                   /note="W -> C (in MC4DN13; mistargeted to the mitochondrial
FT                   matrix; loss of interaction with SCO2 and MT-CO2;
FT                   dbSNP:rs1558123786)"
FT                   /evidence="ECO:0000269|PubMed:24549041,
FT                   ECO:0000269|PubMed:25959673"
FT                   /id="VAR_075046"
FT   VARIANT         66
FT                   /note="W -> R (in MC4DN13; dbSNP:rs875989827)"
FT                   /evidence="ECO:0000269|PubMed:25339201"
FT                   /id="VAR_075047"
FT   HELIX           53..71
FT                   /evidence="ECO:0007829|PDB:6PCE"
FT   TURN            72..74
FT                   /evidence="ECO:0007829|PDB:6PCE"
FT   HELIX           76..78
FT                   /evidence="ECO:0007829|PDB:6PCE"
FT   HELIX           80..89
FT                   /evidence="ECO:0007829|PDB:6PCE"
FT   HELIX           92..108
FT                   /evidence="ECO:0007829|PDB:6PCE"
FT   HELIX           112..116
FT                   /evidence="ECO:0007829|PDB:6PCE"
FT   INIT_MET        Q5JTJ3-3:1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         Q5JTJ3-3:2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
SQ   SEQUENCE   125 AA;  14116 MW;  69192034A460F462 CRC64;
     MGPGGPLLSP SRGFLLCKTG WHSNRLLGDC GPHTPVSTAL SFIAVGMAAP SMKERQVCWG
     ARDEYWKCLD ENLEDASQCK KLRSSFESSC PQQWIKYFDK RRDYLKFKEK FEAGQFEPSE
     TTAKS
//