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HIG1A_RAT
ID   HIG1A_RAT               Reviewed;          93 AA.
AC   Q8VH49; Q6PCV5;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 2.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=HIG1 domain family member 1A, mitochondrial;
DE   AltName: Full=Hypoxia-inducible gene 1 protein;
GN   Name=Higd1a; Synonyms=Hig1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC   STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RX   PubMed=15968589; DOI=10.1387/ijdb.041901gb;
RA   Bedo G.R., Vargas M., Ferreiro M.J., Chalar C., Agrati D.;
RT   "Characterization of hypoxia induced gene 1: expression during rat central
RT   nervous system maturation and evidence of antisense RNA expression.";
RL   Int. J. Dev. Biol. 49:431-436(2005).
RN   [2]
RP   SEQUENCE REVISION TO 8.
RC   STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA   Vargas M., Bedo G.;
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pituitary;
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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Associates with cytochrome c oxidase (COX, complex IV);
CC       proposed complex component. Also associates with respiratory chain
CC       supercomplexes (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00836}; Multi-pass membrane protein {ECO:0000255|PROSITE-
CC       ProRule:PRU00836}. Mitochondrion inner membrane {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in brain and spinal cord.
CC       {ECO:0000269|PubMed:15968589}.
CC   -!- DEVELOPMENTAL STAGE: Expression is increased between P1 and P15 in the
CC       spinal cord and a differential spatial pattern. In the P1 spinal cord
CC       there is a preferential expression in regions of dorsal laminae II and
CC       III and laminae IX ventrally; while in P8, the distribution is more
CC       widespread and overall expression is increased.
CC       {ECO:0000269|PubMed:15968589}.
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DR   EMBL; AY062253; AAL38979.2; -; mRNA.
DR   EMBL; BC059118; AAH59118.1; -; mRNA.
DR   RefSeq; NP_543178.2; NM_080902.4.
DR   AlphaFoldDB; Q8VH49; -.
DR   SMR; Q8VH49; -.
DR   STRING; 10116.ENSRNOP00000061362; -.
DR   iPTMnet; Q8VH49; -.
DR   PhosphoSitePlus; Q8VH49; -.
DR   jPOST; Q8VH49; -.
DR   PaxDb; Q8VH49; -.
DR   PRIDE; Q8VH49; -.
DR   Ensembl; ENSRNOT00000064114; ENSRNOP00000061362; ENSRNOG00000019428.
DR   GeneID; 140937; -.
DR   KEGG; rno:140937; -.
DR   UCSC; RGD:620215; rat.
DR   CTD; 25994; -.
DR   RGD; 620215; Higd1a.
DR   eggNOG; KOG4431; Eukaryota.
DR   GeneTree; ENSGT00940000154276; -.
DR   HOGENOM; CLU_153308_2_0_1; -.
DR   InParanoid; Q8VH49; -.
DR   OMA; GYSMAKE; -.
DR   OrthoDB; 1581485at2759; -.
DR   PhylomeDB; Q8VH49; -.
DR   PRO; PR:Q8VH49; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000019428; Expressed in duodenum and 20 other tissues.
DR   Genevisible; Q8VH49; RN.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; ISO:RGD.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISO:RGD.
DR   GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0042149; P:cellular response to glucose starvation; ISO:RGD.
DR   GO; GO:0071456; P:cellular response to hypoxia; ISO:RGD.
DR   GO; GO:0097250; P:mitochondrial respirasome assembly; IBA:GO_Central.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR   GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; ISO:RGD.
DR   GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISO:RGD.
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   Acetylation; Electron transport; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Phosphoprotein; Reference proteome;
KW   Respiratory chain; Transmembrane; Transmembrane helix; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y241"
FT   CHAIN           2..93
FT                   /note="HIG1 domain family member 1A, mitochondrial"
FT                   /id="PRO_0000215773"
FT   TRANSMEM        28..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00836"
FT   TRANSMEM        69..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00836"
FT   TOPO_DOM        90..93
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          2..93
FT                   /note="HIG1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00836"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y241"
FT   MOD_RES         8
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   93 AA;  10301 MW;  27E879D784C0A8C9 CRC64;
     MSTNTDLSLS SYDEGQGSKF IRKARETPFV PIGMAGFAAI VAYGLYKLKS RGNTKMSIHL
     IHMRVAAQGF VVGAMTLGMG YSMYQEFWAK RKP
 
 
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