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MIC26_BOVIN
ID   MIC26_BOVIN             Reviewed;         198 AA.
AC   Q148H0;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=MICOS complex subunit MIC26;
DE   AltName: Full=Apolipoprotein O;
DE   AltName: Full=MICOS complex subunit MIC23;
DE   AltName: Full=Protein FAM121B;
DE   Flags: Precursor;
GN   Name=APOO; Synonyms=FAM121B, MIC23, MIC26;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the MICOS complex, a large protein complex of
CC       the mitochondrial inner membrane that plays crucial roles in the
CC       maintenance of crista junctions, inner membrane architecture, and
CC       formation of contact sites to the outer membrane. Plays a crucial role
CC       in crista junction formation and mitochondrial function. Can induce
CC       cardiac lipotoxicity by enhancing mitochondrial respiration and fatty
CC       acid metabolism in cardiac myoblasts. Promotes cholesterol efflux from
CC       macrophage cells. Detected in HDL, LDL and VLDL. Secreted by a
CC       microsomal triglyceride transfer protein (MTTP)-dependent mechanism,
CC       probably as a VLDL-associated protein that is subsequently transferred
CC       to HDL. {ECO:0000250|UniProtKB:Q9BUR5}.
CC   -!- SUBUNIT: Component of the mitochondrial contact site and cristae
CC       organizing system (MICOS) complex, composed of at least MICOS10/MIC10,
CC       CHCHD3/MIC19, CHCHD6/MIC25, APOOL/MIC27, IMMT/MIC60, APOO/MIC23/MIC26
CC       and MICOS13/MIC13. This complex was also known under the names MINOS or
CC       MitOS complex. The MICOS complex associates with mitochondrial outer
CC       membrane proteins SAMM50, MTX1 and MTX2 (together described as
CC       components of the mitochondrial outer membrane sorting assembly
CC       machinery (SAM) complex) and DNAJC11, mitochondrial inner membrane
CC       protein TMEM11 and with HSPA9. The MICOS and SAM complexes together
CC       with DNAJC11 are part of a large protein complex spanning both
CC       membranes termed the mitochondrial intermembrane space bridging (MIB)
CC       complex. Interacts with IMMT/MIC60. Interacts with MICOS10/MIC10 and
CC       APOOL/MIC27. {ECO:0000250|UniProtKB:Q9BUR5}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:Q9BUR5}; Single-pass membrane protein
CC       {ECO:0000255}. Secreted {ECO:0000250|UniProtKB:Q9BUR5}. Mitochondrion
CC       {ECO:0000250|UniProtKB:Q9BUR5}. Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q9BUR5}. Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:Q9BUR5}. Note=Exists in three distinct forms: a
CC       glycosylated and secreted form, an ER/Golgi-resident form and a non-
CC       glycosylated mitochondrial form. {ECO:0000250|UniProtKB:Q9BUR5}.
CC   -!- PTM: O-glycosylation; glycosaminoglycan of chondroitin-sulfate type.
CC       {ECO:0000250|UniProtKB:Q9BUR5}.
CC   -!- SIMILARITY: Belongs to the apolipoprotein O/MICOS complex subunit Mic27
CC       family. {ECO:0000305}.
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DR   EMBL; BC118339; AAI18340.1; -; mRNA.
DR   RefSeq; NP_001069107.1; NM_001075639.1.
DR   AlphaFoldDB; Q148H0; -.
DR   STRING; 9913.ENSBTAP00000014525; -.
DR   PaxDb; Q148H0; -.
DR   Ensembl; ENSBTAT00000014525; ENSBTAP00000014525; ENSBTAG00000010937.
DR   GeneID; 513847; -.
DR   KEGG; bta:513847; -.
DR   CTD; 79135; -.
DR   VEuPathDB; HostDB:ENSBTAG00000010937; -.
DR   VGNC; VGNC:26035; APOO.
DR   eggNOG; KOG4798; Eukaryota.
DR   GeneTree; ENSGT00530000063666; -.
DR   InParanoid; Q148H0; -.
DR   OMA; YTSWCQD; -.
DR   OrthoDB; 1605767at2759; -.
DR   Proteomes; UP000009136; Chromosome X.
DR   Bgee; ENSBTAG00000010937; Expressed in oocyte and 103 other tissues.
DR   ExpressionAtlas; Q148H0; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR   GO; GO:0034364; C:high-density lipoprotein particle; IEA:UniProtKB-KW.
DR   GO; GO:0031305; C:integral component of mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0034362; C:low-density lipoprotein particle; IEA:UniProtKB-KW.
DR   GO; GO:0061617; C:MICOS complex; ISS:UniProtKB.
DR   GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-KW.
DR   GO; GO:0042407; P:cristae formation; ISS:UniProtKB.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   InterPro; IPR019166; MIC26/MIC27.
DR   InterPro; IPR033182; MIC26/MIC27_animal.
DR   PANTHER; PTHR14564; PTHR14564; 1.
DR   Pfam; PF09769; ApoO; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Glycoprotein; Golgi apparatus; HDL; LDL;
KW   Lipid transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Proteoglycan; Reference proteome; Secreted; Signal; Transmembrane;
KW   Transmembrane helix; Transport; VLDL.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..198
FT                   /note="MICOS complex subunit MIC26"
FT                   /id="PRO_0000254645"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        162
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   198 AA;  22562 MW;  C670030227E398F9 CRC64;
     MFKVIHRYVG PASLSLLTFK VYASSKKDSP HKDTVKVNEL SLYSVPEHQS KYVEEPRTQL
     EESISHLRHY CEPYTSWCQE KYSQNKPKIQ SLVQWGLDSY EYLQNAPPGF FPRLGVIGFA
     GVVGLVLARG SKIKKLVYPP GFMGFAASLY YPQQAIVFVQ VSGEKLYDWG LRGYIVVEDL
     WKENFQKSGN VKNSPGNK
 
 
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