ATPMK_RAT
ID ATPMK_RAT Reviewed; 58 AA.
AC Q9JJW3;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=ATP synthase membrane subunit K, mitochondrial;
DE AltName: Full=ATP synthase membrane subunit DAPIT, mitochondrial {ECO:0000305};
DE AltName: Full=Diabetes-associated protein in insulin-sensitive tissues;
DE AltName: Full=Up-regulated during skeletal muscle growth protein 5 {ECO:0000305};
GN Name=Atp5mk; Synonyms=Atp5md {ECO:0000312|RGD:631426}, Dapit, Usmg5;
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], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Skeletal muscle;
RX PubMed=11757806; DOI=10.1007/s005920170018;
RA Paivarinne H., Kainulainen H.;
RT "DAPIT, a novel protein down-regulated in insulin-sensitive tissues in
RT streptozotocin-induced diabetes.";
RL Acta Diabetol. 38:83-86(2001).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE ATP SYNTHASE
RP COMPLEX.
RX PubMed=17575325; DOI=10.1074/mcp.m700097-mcp200;
RA Meyer B., Wittig I., Trifilieff E., Karas M., Schaegger H.;
RT "Identification of two proteins associated with mammalian ATP synthase.";
RL Mol. Cell. Proteomics 6:1690-1699(2007).
CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or
CC Complex V) produces ATP from ADP in the presence of a proton gradient
CC across the membrane which is generated by electron transport complexes
CC of the respiratory chain. F-type ATPases consist of two structural
CC domains, F(1) - containing the extramembraneous catalytic core and F(0)
CC - containing the membrane proton channel, linked together by a central
CC stalk and a peripheral stalk. During catalysis, ATP synthesis in the
CC catalytic domain of F(1) is coupled via a rotary mechanism of the
CC central stalk subunits to proton translocation. ATP5MK is a minor
CC subunit of the mitochondrial membrane ATP synthase required for
CC dimerization of the ATP synthase complex and as such regulates ATP
CC synthesis in the mitochondria. {ECO:0000250|UniProtKB:Q96IX5}.
CC -!- SUBUNIT: Component of an ATP synthase complex composed of ATP5PB,
CC ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8,
CC ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and ATP5MJ
CC (By similarity). The ATP synthase complex/complex V exists as a
CC monomeric and a dimeric supercomplex that helps shape mitochondrial
CC cristae to optimize proton flow. {ECO:0000250|UniProtKB:Q3ZBI7,
CC ECO:0000250|UniProtKB:Q96IX5}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000250|UniProtKB:Q96IX5}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in skeletal and
CC cardiac muscle. Moderately expressed in brain, thymus, stomach and
CC testis. Lowest expression levels were detected in lung, liver, kidney,
CC adrenal gland, spleen, small intestine and adipose tissue. In
CC streptozotocin-induced diabetes, the insulin-sensitive tissues skeletal
CC and cardiac muscle were down-regulated. {ECO:0000269|PubMed:11757806}.
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DR EMBL; AJ271158; CAB71156.1; -; mRNA.
DR RefSeq; NP_598228.1; NM_133544.1.
DR RefSeq; XP_008766441.1; XM_008768219.2.
DR RefSeq; XP_008773622.1; XM_008775400.2.
DR AlphaFoldDB; Q9JJW3; -.
DR SMR; Q9JJW3; -.
DR BioGRID; 251083; 1.
DR IntAct; Q9JJW3; 1.
DR MINT; Q9JJW3; -.
DR STRING; 10116.ENSRNOP00000027496; -.
DR iPTMnet; Q9JJW3; -.
DR PhosphoSitePlus; Q9JJW3; -.
DR SwissPalm; Q9JJW3; -.
DR PaxDb; Q9JJW3; -.
DR PRIDE; Q9JJW3; -.
DR Ensembl; ENSRNOT00000027496; ENSRNOP00000027496; ENSRNOG00000020296.
DR Ensembl; ENSRNOT00000100748; ENSRNOP00000093868; ENSRNOG00000067471.
DR GeneID; 103693430; -.
DR GeneID; 171069; -.
DR KEGG; rno:103693430; -.
DR KEGG; rno:171069; -.
DR CTD; 84833; -.
DR RGD; 631426; Atp5md.
DR VEuPathDB; HostDB:ENSRNOG00000042869; -.
DR eggNOG; ENOG502S82X; Eukaryota.
DR GeneTree; ENSGT00390000015489; -.
DR HOGENOM; CLU_209345_1_0_1; -.
DR InParanoid; Q9JJW3; -.
DR OMA; GIAKHFN; -.
DR OrthoDB; 1629213at2759; -.
DR PhylomeDB; Q9JJW3; -.
DR TreeFam; TF324671; -.
DR PRO; PR:Q9JJW3; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000020296; Expressed in lung and 8 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR InterPro; IPR009125; ATPMK.
DR PANTHER; PTHR34038; PTHR34038; 1.
DR Pfam; PF14960; ATP_synth_reg; 1.
DR PRINTS; PR01821; DAPIT.
PE 1: Evidence at protein level;
KW Acetylation; Membrane; Mitochondrion; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..58
FT /note="ATP synthase membrane subunit K, mitochondrial"
FT /id="PRO_0000231580"
FT TRANSMEM 23..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 16
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q78IK2"
FT MOD_RES 17
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q78IK2"
SQ SEQUENCE 58 AA; 6408 MW; 2CF25C1922534BE6 CRC64;
MAGPESDGQF QFTGIKKYFN SYTLTGRMNC VLATYGGIAL LVLYFKLRPK KTPAVKAT
