SURF1_MOUSE
ID SURF1_MOUSE Reviewed; 306 AA.
AC P09925; Q99KB4; Q9DCU5;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Surfeit locus protein 1;
GN Name=Surf1; Synonyms=Surf-1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3025660; DOI=10.1128/mcb.6.12.4558-4569.1986;
RA Williams T.J., Fried M.;
RT "The MES-1 murine enhancer element is closely associated with the
RT heterogeneous 5' ends of two divergent transcription units.";
RL Mol. Cell. Biol. 6:4558-4569(1986).
RN [2]
RP SEQUENCE REVISION.
RA Fried M.;
RL Submitted (SEP-1988) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=17210671; DOI=10.1093/hmg/ddl477;
RA Dell'agnello C., Leo S., Agostino A., Szabadkai G., Tiveron C., Zulian A.,
RA Prelle A., Roubertoux P., Rizzuto R., Zeviani M.;
RT "Increased longevity and refractoriness to Ca(2+)-dependent
RT neurodegeneration in Surf1 knockout mice.";
RL Hum. Mol. Genet. 16:431-444(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=21167962; DOI=10.1016/j.mito.2010.12.011;
RA Stettner G.M., Viscomi C., Zeviani M., Wilichowski E., Dutschmann M.;
RT "Hypoxic and hypercapnic challenges unveil respiratory vulnerability of
RT Surf1 knockout mice, an animal model of Leigh syndrome.";
RL Mitochondrion 11:413-420(2011).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23838831; DOI=10.1038/jcbfm.2013.116;
RA Lin A.L., Pulliam D.A., Deepa S.S., Halloran J.J., Hussong S.A.,
RA Burbank R.R., Bresnen A., Liu Y., Podlutskaya N., Soundararajan A.,
RA Muir E., Duong T.Q., Bokov A.F., Viscomi C., Zeviani M., Richardson A.G.,
RA Van Remmen H., Fox P.T., Galvan V.;
RT "Decreased in vitro mitochondrial function is associated with enhanced
RT brain metabolism, blood flow, and memory in Surf1-deficient mice.";
RL J. Cereb. Blood Flow Metab. 33:1605-1611(2013).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24911525; DOI=10.1042/bj20140291;
RA Pulliam D.A., Deepa S.S., Liu Y., Hill S., Lin A.L., Bhattacharya A.,
RA Shi Y., Sloane L., Viscomi C., Zeviani M., Van Remmen H.;
RT "Complex IV-deficient Surf1(-/-) mice initiate mitochondrial stress
RT responses.";
RL Biochem. J. 462:359-371(2014).
CC -!- FUNCTION: Component of the MITRAC (mitochondrial translation regulation
CC assembly intermediate of cytochrome c oxidase complex) complex (By
CC similarity). Regulates cytochrome c oxidase assembly (PubMed:17210671,
CC PubMed:23838831, PubMed:24911525). {ECO:0000250|UniProtKB:Q15526,
CC ECO:0000269|PubMed:17210671, ECO:0000269|PubMed:23838831,
CC ECO:0000269|PubMed:24911525}.
CC -!- SUBUNIT: Component of the MITRAC (mitochondrial translation regulation
CC assembly intermediate of cytochrome c oxidase complex) complex, the
CC core components of this complex being COA3/MITRAC12 and COX14.
CC Interacts with COA3. {ECO:0000250|UniProtKB:Q15526}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000269|PubMed:17210671}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Results in smaller animals with mild decreased
CC motor skills, enhanced working spatial and recognition memory, and
CC increased longevity (PubMed:17210671, PubMed:23838831,
CC PubMed:24911525). Increases global and regional cerebral blood flow
CC (PubMed:23838831). Increases lactate levels in blood and brain, and
CC increases glucose consumption in the brain (PubMed:17210671,
CC PubMed:23838831, PubMed:24911525). Increases hydrogen peroxide
CC production and succinate dehydrogenase (SDH) activity, but decreases
CC COX activity and respiration (PubMed:17210671, PubMed:21167962,
CC PubMed:23838831, PubMed:24911525). In the brain, increases Hif1a and
CC phosphorylated cyclic AMP response element-binding protein levels
CC (PubMed:23838831). In the brain, increases resistance to calcium-
CC related excitotoxic brain damage (PubMed:17210671). In skeletal
CC muscles, results in mitochondrial unfolded protein response
CC (PubMed:24911525). In the heart, results in elevated Nfe2l2 and Hmox1
CC expression (PubMed:24911525). Primary cultures of mutant neuronal cells
CC show reduced sensitivity to glutamate-induced cytosolic calcium signal
CC and impaired mitochondrial calcium uptake without changing the
CC mitochondrial structure and membrane potential (PubMed:17210671).
CC Primary cultures of phrenic and central vagus nerves show increased
CC respiratory frequency and altered response to systemic hypoxia and
CC hypercapnia (PubMed:21167962). {ECO:0000269|PubMed:17210671,
CC ECO:0000269|PubMed:21167962, ECO:0000269|PubMed:23838831,
CC ECO:0000269|PubMed:24911525}.
CC -!- SIMILARITY: Belongs to the SURF1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M14689; AAA40153.1; -; Genomic_DNA.
DR EMBL; AK002469; BAB22123.1; -; mRNA.
DR EMBL; BC004755; AAH04755.1; -; mRNA.
DR CCDS; CCDS50543.1; -.
DR PIR; B25394; B25394.
DR RefSeq; NP_001258653.2; NM_001271724.1.
DR RefSeq; NP_038705.2; NM_013677.2.
DR AlphaFoldDB; P09925; -.
DR STRING; 10090.ENSMUSP00000015934; -.
DR iPTMnet; P09925; -.
DR PhosphoSitePlus; P09925; -.
DR SwissPalm; P09925; -.
DR EPD; P09925; -.
DR jPOST; P09925; -.
DR MaxQB; P09925; -.
DR PaxDb; P09925; -.
DR PRIDE; P09925; -.
DR ProteomicsDB; 254781; -.
DR Antibodypedia; 18363; 169 antibodies from 29 providers.
DR Ensembl; ENSMUST00000015934; ENSMUSP00000015934; ENSMUSG00000015790.
DR GeneID; 20930; -.
DR KEGG; mmu:20930; -.
DR UCSC; uc008iwh.2; mouse.
DR CTD; 6834; -.
DR MGI; MGI:98443; Surf1.
DR VEuPathDB; HostDB:ENSMUSG00000015790; -.
DR eggNOG; KOG1563; Eukaryota.
DR GeneTree; ENSGT00530000064194; -.
DR InParanoid; P09925; -.
DR OMA; WYSRDVA; -.
DR OrthoDB; 923657at2759; -.
DR Reactome; R-MMU-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-MMU-611105; Respiratory electron transport.
DR Reactome; R-MMU-9707564; Cytoprotection by HMOX1.
DR BioGRID-ORCS; 20930; 7 hits in 71 CRISPR screens.
DR ChiTaRS; Surf1; mouse.
DR PRO; PR:P09925; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P09925; protein.
DR Bgee; ENSMUSG00000015790; Expressed in facial nucleus and 251 other tissues.
DR ExpressionAtlas; P09925; baseline and differential.
DR Genevisible; P09925; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IMP:UniProtKB.
DR GO; GO:0033617; P:mitochondrial cytochrome c oxidase assembly; ISS:UniProtKB.
DR CDD; cd06662; SURF1; 1.
DR InterPro; IPR002994; Surf1/Shy1.
DR InterPro; IPR045214; Surf1/Surf4.
DR PANTHER; PTHR23427; PTHR23427; 1.
DR Pfam; PF02104; SURF1; 1.
DR PROSITE; PS50895; SURF1; 1.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..306
FT /note="Surfeit locus protein 1"
FT /id="PRO_0000215653"
FT TRANSMEM 68..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 9
FT /note="V -> G (in Ref. 1; AAA40153)"
FT /evidence="ECO:0000305"
FT CONFLICT 14
FT /note="M -> I (in Ref. 3; BAB22123)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="W -> CR (in Ref. 1; AAA40153)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 306 AA; 34798 MW; 8D9ECE9FB726AEB7 CRC64;
MAAVMALAVL PRRMTRWSQW AYAGRAQFCA VRRSVFGFSV RSGMVCRPRR CCSSTAETAA
AKAEDDSFLQ WFLLLIPATA FGLGTWQVQR RKWKLKLIAE LESRVMAEPI PLPADPMELK
NLEYRPVKVR GHFDHSKELY IMPRTMVDPV REARDAGRLS STESGAHVVT PFHCSDLGVT
ILVNRGFVPR KKVNPETRQK GQVLGEVDLV GIVRLTENRK PFVPENSPER NHWYYRDLEA
MAKITGADPI FIDADFHSTA PGGPIGGQTR VTLRNEHMQY ILTWYGLCAA TSYLWFQKFV
RRTPIM
