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S41A3_MOUSE
ID   S41A3_MOUSE             Reviewed;         488 AA.
AC   Q921R8; Q9DC67;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Solute carrier family 41 member 3;
GN   Name=Slc41a3;
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] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Heart;
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 MRNA] (ISOFORM 1).
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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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).
CC   -!- FUNCTION: Na(+)/Mg(2+) ion exchanger that acts as a predominant Mg(2+)
CC       efflux system at the mitochondrial inner membrane.
CC       {ECO:0000250|UniProtKB:Q96GZ6}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Mg(2+)(in) + 2 Na(+)(out) = Mg(2+)(out) + 2 Na(+)(in);
CC         Xref=Rhea:RHEA:66616, ChEBI:CHEBI:18420, ChEBI:CHEBI:29101;
CC         Evidence={ECO:0000250|UniProtKB:Q96GZ6};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66617;
CC         Evidence={ECO:0000250|UniProtKB:Q96GZ6};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:Q96GZ6}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q921R8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q921R8-2; Sequence=VSP_026939;
CC   -!- SIMILARITY: Belongs to the SLC41A transporter family. {ECO:0000305}.
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DR   EMBL; AK003140; BAB22598.1; -; mRNA.
DR   EMBL; BC011108; AAH11108.1; -; mRNA.
DR   CCDS; CCDS20362.1; -. [Q921R8-1]
DR   CCDS; CCDS20363.1; -. [Q921R8-2]
DR   RefSeq; NP_001032570.1; NM_001037493.2. [Q921R8-2]
DR   RefSeq; NP_082144.2; NM_027868.2.
DR   AlphaFoldDB; Q921R8; -.
DR   IntAct; Q921R8; 1.
DR   MINT; Q921R8; -.
DR   STRING; 10090.ENSMUSP00000037473; -.
DR   PhosphoSitePlus; Q921R8; -.
DR   MaxQB; Q921R8; -.
DR   PaxDb; Q921R8; -.
DR   PeptideAtlas; Q921R8; -.
DR   PRIDE; Q921R8; -.
DR   ProteomicsDB; 256819; -. [Q921R8-1]
DR   ProteomicsDB; 256820; -. [Q921R8-2]
DR   Antibodypedia; 33042; 39 antibodies from 14 providers.
DR   DNASU; 71699; -.
DR   Ensembl; ENSMUST00000032177; ENSMUSP00000032177; ENSMUSG00000030089. [Q921R8-2]
DR   GeneID; 71699; -.
DR   KEGG; mmu:71699; -.
DR   UCSC; uc009cxp.2; mouse. [Q921R8-2]
DR   CTD; 54946; -.
DR   MGI; MGI:1918949; Slc41a3.
DR   VEuPathDB; HostDB:ENSMUSG00000030089; -.
DR   eggNOG; KOG3788; Eukaryota.
DR   GeneTree; ENSGT00950000183042; -.
DR   HOGENOM; CLU_018207_2_0_1; -.
DR   InParanoid; Q921R8; -.
DR   OMA; FCFQGKK; -.
DR   OrthoDB; 1059294at2759; -.
DR   PhylomeDB; Q921R8; -.
DR   BioGRID-ORCS; 71699; 3 hits in 72 CRISPR screens.
DR   PRO; PR:Q921R8; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q921R8; protein.
DR   Bgee; ENSMUSG00000030089; Expressed in interventricular septum and 222 other tissues.
DR   ExpressionAtlas; Q921R8; baseline and differential.
DR   Genevisible; Q921R8; MM.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0061768; F:magnesium:sodium antiporter activity; ISS:UniProtKB.
DR   GO; GO:0045016; P:mitochondrial magnesium ion transmembrane transport; ISS:UniProtKB.
DR   Gene3D; 1.10.357.20; -; 2.
DR   InterPro; IPR006667; SLC41_membr_dom.
DR   InterPro; IPR036739; SLC41_membr_dom_sf.
DR   InterPro; IPR045349; SLC41A1-3.
DR   PANTHER; PTHR16228; PTHR16228; 1.
DR   Pfam; PF01769; MgtE; 2.
DR   SUPFAM; SSF161093; SSF161093; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Ion transport; Magnesium; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..488
FT                   /note="Solute carrier family 41 member 3"
FT                   /id="PRO_0000295593"
FT   TRANSMEM        63..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        147..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        189..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        220..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        251..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        284..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        377..397
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        406..426
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        450..470
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..90
FT                   /note="MEGTEARQRRLEGCGRLKELGPLPSHDAGRLPKASEEGHLAVSESQLVDAKS
FT                   LEAPPGRETSLIIGFQVVIPFLLAGVGLSWAGLLLNYF -> MVVTQLSLEFRFQGKKL
FT                   RGFSCELTRSPHGILPEPVLTTTCQVAIPILLSGLGMMTAGLVMNTV (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_026939"
SQ   SEQUENCE   488 AA;  53257 MW;  E43401605DC1EEC0 CRC64;
     MEGTEARQRR LEGCGRLKEL GPLPSHDAGR LPKASEEGHL AVSESQLVDA KSLEAPPGRE
     TSLIIGFQVV IPFLLAGVGL SWAGLLLNYF QHWPVFKDVK DLMTLVPPLV GLKGNLEMTL
     ASRLSTSANT GQIDDRQERY KIISSNLAVV QVQATVVGLL AAVASLMLGT VSHEEFDWSK
     VALLCTSSVI TAFLAALALG ILMICIVIGA RKFGVNPDNI ATPIAASLGD LITLSILALM
     SSFFYSHKDT WYLTPLVCVG FLALTPLWLF IAKQNPPIMK ILKYGWFPII LAMIISSFGG
     LILSKTISKH EFKGMAVLTP VMCGVGGNLV AIQTSRISTF LHMWSTPGVL PVQMKRFWPN
     PCFIFCSSEI NSVSARVLLF LVVPGHLIFF YLICLVEGQS VTNSKIFILL YLVAGVVQVV
     ILLYLAEVTV RLTWHQALDP DNHCIPYLTG LGDLLGTSLL ALCFFLDWLL RGRANLQELV
     SELVSVPP
 
 
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