ID A0A0H2UHI7_RAT Unreviewed; 403 AA.
AC A0A0H2UHI7;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Outer mitochondrial transmembrane helix translocase {ECO:0000256|ARBA:ARBA00040718};
GN Name=Atad1 {ECO:0000313|Ensembl:ENSRNOP00000014684.5,
GN ECO:0000313|RGD:1308570};
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 {ECO:0000313|Ensembl:ENSRNOP00000014684.5, ECO:0000313|Proteomes:UP000002494};
RN [1] {ECO:0000313|Ensembl:ENSRNOP00000014684.5, ECO:0000313|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000014684.5,
RC ECO:0000313|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RG Rat Genome Sequencing Project Consortium;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0000313|Ensembl:ENSRNOP00000014684.5}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000014684.5};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-with a C-terminal TM segment(out) + ATP + H2O =
CC [protein]-with a C-terminal TM segment(in) + ADP + H(+) + phosphate;
CC Xref=Rhea:RHEA:66168, Rhea:RHEA-COMP:16963, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:90782, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00036758};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC outer membrane {ECO:0000256|ARBA:ARBA00004572}; Single-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004572}. Postsynaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00037805}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00037805}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. MSP1 subfamily.
CC {ECO:0000256|ARBA:ARBA00038383}.
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DR AlphaFoldDB; A0A0H2UHI7; -.
DR SMR; A0A0H2UHI7; -.
DR jPOST; A0A0H2UHI7; -.
DR Ensembl; ENSRNOT00000014684.8; ENSRNOP00000014684.5; ENSRNOG00000010861.8.
DR RGD; 1308570; Atad1.
DR GeneTree; ENSGT00940000165544; -.
DR OMA; CRNAAMR; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000010861; Expressed in testis and 19 other cell types or tissues.
DR ExpressionAtlas; A0A0H2UHI7; baseline and differential.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd19520; RecA-like_ATAD1; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR45644; AAA ATPASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G12920)-RELATED-RELATED; 1.
DR PANTHER; PTHR45644:SF2; OUTER MITOCHONDRIAL TRANSMEMBRANE HELIX TRANSLOCASE; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|RuleBase:RU003651};
KW Membrane {ECO:0000256|ARBA:ARBA00022787};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00022787};
KW Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A0H2UHI7};
KW Reference proteome {ECO:0000313|Proteomes:UP000002494}.
FT DOMAIN 167..303
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 403 AA; 45091 MW; 898DCF074D491CBE CRC64;
MLRAGAGLQP PEAFSPRPHF FPVRGRANAS VVSGLTSGLT IKMVHAEAFS RPLSRNEVVG
LIFRLTIFGA VTYFTIKWMV DAIDPTRKQK VEAQKQAEKL MKQIGVKNVK LSEYEMSIAA
HLVDPLNMHV TWSDIAGLDD VITDLKDTVI LPIKKKHLFE NSRLLQPPKG VLLYGPPGCG
KTLIAKATAK EAGCRFINLQ PSTLTDKWYG ESQKLAAAVF SLAIKLQPSI IFIDEIDSFL
RNRSSSDHEA TAMMKAQFMS LWDGLDTDHS CQVIVMGATN RPQDLDSAIM RRMPTRFHIN
QPALKQREAI LKLILKNENV DRHVDLLEVA QETDGFSGSD LKEMCRDAAL LCVREYVNST
SEESHDEDEI RPVQQQDLHR AIEKMKKSKD AAFQSVLTHV CLD
//
