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S2533_MOUSE
ID   S2533_MOUSE             Reviewed;         320 AA.
AC   Q3TZX3; Q921P8; Q9CYJ1;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Solute carrier family 25 member 33;
GN   Name=Slc25a33;
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Spleen;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
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   SUBCELLULAR LOCATION, AND FUNCTION.
RX   PubMed=17596519; DOI=10.1091/mbc.e06-12-1109;
RA   Floyd S., Favre C., Lasorsa F.M., Leahy M., Trigiante G., Stroebel P.,
RA   Marx A., Loughran G., O'Callaghan K., Marobbio C.M., Slotboom D.J.,
RA   Kunji E.R., Palmieri F., O'Connor R.;
RT   "The insulin-like growth factor-I-mTOR signaling pathway induces the
RT   mitochondrial pyrimidine nucleotide carrier to promote cell growth.";
RL   Mol. Biol. Cell 18:3545-3555(2007).
CC   -!- FUNCTION: Mitochondrial transporter that imports/exports pyrimidine
CC       nucleotides into and from mitochondria. Transports preferentially
CC       uracil, thymine, and cytosine (deoxy)nucleoside di- and triphosphates
CC       by an antiport mechanism. Also transports guanine but not adenine
CC       (deoxy)nucleotides. Is inhibited strongly by pyridoxal 5'-phosphate,
CC       4,7-diphenyl-1,10-phenanthroline, tannic acid, and mercurials (mercury
CC       dichloride, mersalyl acid, p-hydroxymercuribenzoate). Participates in
CC       mitochondrial genome maintenance, regulation of mitochondrial membrane
CC       potential and mitochondrial respiration (By similarity). Upon INS or
CC       IGF1 stimulation regulates cell growth and proliferation by controlling
CC       mitochondrial DNA replication and transcription, the ratio of
CC       mitochondria-to nuclear-encoded components of the electron transport
CC       chain resulting in control of mitochondrial ROS production
CC       (PubMed:17596519). Participates in dendritic cell endocytosis and may
CC       associate with mitochondrial oxidative phosphorylation (By similarity).
CC       {ECO:0000250|UniProtKB:Q9BSK2, ECO:0000269|PubMed:17596519}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000305|PubMed:17596519}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB30846.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK017628; BAB30846.1; ALT_FRAME; mRNA.
DR   EMBL; AK157423; BAE34084.1; -; mRNA.
DR   EMBL; AL626808; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC011293; AAH11293.1; -; mRNA.
DR   CCDS; CCDS38976.1; -.
DR   RefSeq; NP_081736.2; NM_027460.2.
DR   AlphaFoldDB; Q3TZX3; -.
DR   SMR; Q3TZX3; -.
DR   BioGRID; 214130; 3.
DR   STRING; 10090.ENSMUSP00000101311; -.
DR   PhosphoSitePlus; Q3TZX3; -.
DR   SwissPalm; Q3TZX3; -.
DR   EPD; Q3TZX3; -.
DR   MaxQB; Q3TZX3; -.
DR   PaxDb; Q3TZX3; -.
DR   PeptideAtlas; Q3TZX3; -.
DR   PRIDE; Q3TZX3; -.
DR   ProteomicsDB; 260763; -.
DR   Antibodypedia; 53479; 76 antibodies from 18 providers.
DR   DNASU; 70556; -.
DR   Ensembl; ENSMUST00000105686; ENSMUSP00000101311; ENSMUSG00000028982.
DR   GeneID; 70556; -.
DR   KEGG; mmu:70556; -.
DR   UCSC; uc008vxe.1; mouse.
DR   CTD; 84275; -.
DR   MGI; MGI:1917806; Slc25a33.
DR   VEuPathDB; HostDB:ENSMUSG00000028982; -.
DR   eggNOG; KOG0757; Eukaryota.
DR   GeneTree; ENSGT00940000158954; -.
DR   HOGENOM; CLU_015166_6_0_1; -.
DR   InParanoid; Q3TZX3; -.
DR   OMA; PTWAVYM; -.
DR   OrthoDB; 1372287at2759; -.
DR   PhylomeDB; Q3TZX3; -.
DR   TreeFam; TF314220; -.
DR   BioGRID-ORCS; 70556; 2 hits in 73 CRISPR screens.
DR   PRO; PR:Q3TZX3; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q3TZX3; protein.
DR   Bgee; ENSMUSG00000028982; Expressed in gastrula and 246 other tissues.
DR   Genevisible; Q3TZX3; MM.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0015218; F:pyrimidine nucleotide transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR   GO; GO:1990314; P:cellular response to insulin-like growth factor stimulus; ISS:UniProtKB.
DR   GO; GO:0031930; P:mitochondria-nucleus signaling pathway; IDA:UniProtKB.
DR   GO; GO:0000002; P:mitochondrial genome maintenance; ISS:UniProtKB.
DR   GO; GO:0034551; P:mitochondrial respiratory chain complex III assembly; ISS:UniProtKB.
DR   GO; GO:0006390; P:mitochondrial transcription; ISS:UniProtKB.
DR   GO; GO:0007005; P:mitochondrion organization; ISS:UniProtKB.
DR   GO; GO:0030307; P:positive regulation of cell growth; IDA:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:1990519; P:pyrimidine nucleotide import into mitochondrion; IMP:UniProtKB.
DR   GO; GO:0006864; P:pyrimidine nucleotide transport; ISS:UniProtKB.
DR   GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISS:UniProtKB.
DR   GO; GO:0002082; P:regulation of oxidative phosphorylation; ISS:UniProtKB.
DR   GO; GO:1903426; P:regulation of reactive oxygen species biosynthetic process; ISS:UniProtKB.
DR   Gene3D; 1.50.40.10; -; 2.
DR   InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR   InterPro; IPR023395; Mt_carrier_dom_sf.
DR   Pfam; PF00153; Mito_carr; 3.
DR   SUPFAM; SSF103506; SSF103506; 1.
DR   PROSITE; PS50920; SOLCAR; 3.
PE   2: Evidence at transcript level;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Repeat; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..320
FT                   /note="Solute carrier family 25 member 33"
FT                   /id="PRO_0000291786"
FT   TRANSMEM        12..32
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        49..65
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        121..141
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        190..210
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        233..253
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        298..318
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          9..118
FT                   /note="Solcar 1"
FT   REPEAT          126..213
FT                   /note="Solcar 2"
FT   REPEAT          231..315
FT                   /note="Solcar 3"
FT   CONFLICT        31
FT                   /note="P -> H (in Ref. 1; BAB30846)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        122
FT                   /note="I -> V (in Ref. 3; AAH11293)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        129
FT                   /note="T -> N (in Ref. 1; BAB30846)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        154
FT                   /note="T -> K (in Ref. 1; BAB30846)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        189
FT                   /note="G -> V (in Ref. 1; BAB30846)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        293
FT                   /note="A -> T (in Ref. 1; BAB30846)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   320 AA;  35064 MW;  39D2EB15037D2AEC CRC64;
     MATGTQQKEN TLLHLFAGGC GGTVGAIFTC PLEVIKTRLQ SSRLALRTVY YPQVHLGTIS
     GAGMVRPTSV TPGLLQVLKS ILEKEGPKSL FRGLGPNLVG VAPSRAVYFA CYSKAKEQFN
     GIFVPNSNTV HILSAGSAAF VTNTLMNPIW MVKTRMQLER KVRGCKQMNT LQCARRVYQT
     EGVRGFYRGL TASYAGISET IICFAIYESL KKCLKDAPIV SSTDGAEKSS SGFFGLMAAA
     AVSKGCASCI AYPHEVIRTR LREEGSKYRS FVQTARLVFR EEGYLAFYRG LFAQLIRQIP
     NTAIVLSTYE FIVYLLGERA
 
 
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