HIG1A_HUMAN
ID HIG1A_HUMAN Reviewed; 93 AA.
AC Q9Y241; Q9UFZ2;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=HIG1 domain family member 1A, mitochondrial;
DE AltName: Full=Hypoxia-inducible gene 1 protein;
DE AltName: Full=RCF1 homolog A;
DE Short=RCF1a;
GN Name=HIGD1A; Synonyms=HIG1; ORFNames=HSPC010;
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 INDUCTION.
RC TISSUE=Cervix carcinoma;
RX PubMed=10690527;
RA Denko N.C., Schindler C., Koong A., Laderoute K., Green C., Giaccia A.J.;
RT "Epigenetic regulation of gene expression in cervical cancer cells by the
RT tumor microenvironment.";
RL Clin. Cancer Res. 6:480-487(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Bone marrow, Brain, Lung, and 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 [6]
RP PROTEIN SEQUENCE OF 2-19 AND 26-47, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [7]
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 [8]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=22342701; DOI=10.1016/j.cmet.2012.01.016;
RA Vukotic M., Oeljeklaus S., Wiese S., Vogtle F.N., Meisinger C., Meyer H.E.,
RA Zieseniss A., Katschinski D.M., Jans D.C., Jakobs S., Warscheid B.,
RA Rehling P., Deckers M.;
RT "Rcf1 mediates cytochrome oxidase assembly and respirasome formation,
RT revealing heterogeneity of the enzyme complex.";
RL Cell Metab. 15:336-347(2012).
RN [9]
RP STRUCTURE BY NMR.
RX PubMed=22609626; DOI=10.1038/nmeth.2033;
RA Klammt C., Maslennikov I., Bayrhuber M., Eichmann C., Vajpai N., Chiu E.J.,
RA Blain K.Y., Esquivies L., Kwon J.H., Balana B., Pieper U., Sali A.,
RA Slesinger P.A., Kwiatkowski W., Riek R., Choe S.;
RT "Facile backbone structure determination of human membrane proteins by NMR
RT spectroscopy.";
RL Nat. Methods 9:834-839(2012).
CC -!- FUNCTION: Proposed subunit of cytochrome c oxidase (COX, complex IV),
CC which is the terminal component of the mitochondrial respiratory chain
CC that catalyzes the reduction of oxygen to water. May play a role in the
CC assembly of respiratory supercomplexes. {ECO:0000269|PubMed:22342701}.
CC -!- SUBUNIT: Associates with cytochrome c oxidase (COX, complex IV);
CC proposed complex component. Also associates with respiratory chain
CC supercomplexes. {ECO:0000269|PubMed:22342701}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00836, ECO:0000269|PubMed:22342701}; Multi-pass membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00836,
CC ECO:0000269|PubMed:22342701}. Mitochondrion inner membrane
CC {ECO:0000305|PubMed:22342701}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y241-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y241-2; Sequence=VSP_041211;
CC -!- INDUCTION: By hypoxia. {ECO:0000269|PubMed:10690527}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BG400624; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF145385; AAD33954.1; -; mRNA.
DR EMBL; AF077034; AAD27767.1; -; mRNA.
DR EMBL; AL110233; CAB53686.1; -; mRNA.
DR EMBL; CR457385; CAG33666.1; -; mRNA.
DR EMBL; BC000601; AAH00601.1; -; mRNA.
DR EMBL; BC009583; AAH09583.1; -; mRNA.
DR EMBL; BC009594; AAH09594.1; -; mRNA.
DR EMBL; BC070277; AAH70277.1; -; mRNA.
DR EMBL; BG400624; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS43073.1; -. [Q9Y241-1]
DR CCDS; CCDS46806.1; -. [Q9Y241-2]
DR PIR; T14766; T14766.
DR RefSeq; NP_001093138.1; NM_001099668.1. [Q9Y241-2]
DR RefSeq; NP_001093139.1; NM_001099669.1. [Q9Y241-1]
DR RefSeq; NP_054775.2; NM_014056.3. [Q9Y241-1]
DR PDB; 2LOM; NMR; -; A=1-93.
DR PDBsum; 2LOM; -.
DR AlphaFoldDB; Q9Y241; -.
DR BMRB; Q9Y241; -.
DR SMR; Q9Y241; -.
DR BioGRID; 117472; 95.
DR IntAct; Q9Y241; 28.
DR MINT; Q9Y241; -.
DR STRING; 9606.ENSP00000398064; -.
DR iPTMnet; Q9Y241; -.
DR PhosphoSitePlus; Q9Y241; -.
DR BioMuta; HIGD1A; -.
DR DMDM; 74753465; -.
DR EPD; Q9Y241; -.
DR jPOST; Q9Y241; -.
DR MassIVE; Q9Y241; -.
DR MaxQB; Q9Y241; -.
DR PaxDb; Q9Y241; -.
DR PeptideAtlas; Q9Y241; -.
DR PRIDE; Q9Y241; -.
DR ProteomicsDB; 85638; -. [Q9Y241-1]
DR ProteomicsDB; 85639; -. [Q9Y241-2]
DR TopDownProteomics; Q9Y241-1; -. [Q9Y241-1]
DR TopDownProteomics; Q9Y241-2; -. [Q9Y241-2]
DR Antibodypedia; 45649; 117 antibodies from 27 providers.
DR DNASU; 25994; -.
DR Ensembl; ENST00000321331.12; ENSP00000319393.7; ENSG00000181061.14. [Q9Y241-1]
DR Ensembl; ENST00000418900.6; ENSP00000402160.2; ENSG00000181061.14. [Q9Y241-1]
DR Ensembl; ENST00000452906.3; ENSP00000398064.2; ENSG00000181061.14. [Q9Y241-2]
DR GeneID; 25994; -.
DR KEGG; hsa:25994; -.
DR MANE-Select; ENST00000321331.12; ENSP00000319393.7; NM_014056.4; NP_054775.2.
DR UCSC; uc003cma.5; human. [Q9Y241-1]
DR CTD; 25994; -.
DR GeneCards; HIGD1A; -.
DR HGNC; HGNC:29527; HIGD1A.
DR HPA; ENSG00000181061; Low tissue specificity.
DR MIM; 618623; gene.
DR neXtProt; NX_Q9Y241; -.
DR OpenTargets; ENSG00000181061; -.
DR PharmGKB; PA142671681; -.
DR VEuPathDB; HostDB:ENSG00000181061; -.
DR eggNOG; KOG4431; Eukaryota.
DR GeneTree; ENSGT00940000154276; -.
DR HOGENOM; CLU_153308_2_0_1; -.
DR InParanoid; Q9Y241; -.
DR OrthoDB; 1581485at2759; -.
DR PhylomeDB; Q9Y241; -.
DR TreeFam; TF314628; -.
DR PathwayCommons; Q9Y241; -.
DR Reactome; R-HSA-1234158; Regulation of gene expression by Hypoxia-inducible Factor.
DR SignaLink; Q9Y241; -.
DR BioGRID-ORCS; 25994; 73 hits in 1038 CRISPR screens.
DR ChiTaRS; HIGD1A; human.
DR GeneWiki; HIGD1A; -.
DR GenomeRNAi; 25994; -.
DR Pharos; Q9Y241; Tbio.
DR PRO; PR:Q9Y241; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9Y241; protein.
DR Bgee; ENSG00000181061; Expressed in rectum and 160 other tissues.
DR ExpressionAtlas; Q9Y241; baseline and differential.
DR Genevisible; Q9Y241; 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:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0032991; C:protein-containing complex; IDA:LIFEdb.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0097250; P:mitochondrial respirasome assembly; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:MGI.
DR InterPro; IPR007667; Hypoxia_induced_domain.
DR Pfam; PF04588; HIG_1_N; 1.
DR PROSITE; PS51503; HIG1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing;
KW Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Phosphoprotein; Reference proteome; Respiratory chain; Stress response;
KW Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.6"
FT CHAIN 2..93
FT /note="HIG1 domain family member 1A, mitochondrial"
FT /id="PRO_0000215770"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00836"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00836"
FT DOMAIN 1..93
FT /note="HIG1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00836"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.6"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VH49"
FT VAR_SEQ 1
FT /note="M -> MEQKLVEEILQAITM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_041211"
FT CONFLICT 92
FT /note="K -> E (in Ref. 3; CAB53686 and 4; CAG33666)"
FT /evidence="ECO:0000305"
FT HELIX 17..21
FT /evidence="ECO:0007829|PDB:2LOM"
FT HELIX 30..48
FT /evidence="ECO:0007829|PDB:2LOM"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:2LOM"
FT HELIX 65..81
FT /evidence="ECO:0007829|PDB:2LOM"
SQ SEQUENCE 93 AA; 10143 MW; 9399D8D1D381B66B CRC64;
MSTDTGVSLP SYEEDQGSKL IRKAKEAPFV PVGIAGFAAI VAYGLYKLKS RGNTKMSIHL
IHMRVAAQGF VVGAMTVGMG YSMYREFWAK PKP
