ID S41A2_MOUSE Reviewed; 573 AA.
AC Q8BYR8;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 136.
DE RecName: Full=Solute carrier family 41 member 2;
GN Name=Slc41a2;
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; TISSUE=Hypothalamus;
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 FUNCTION, TRANSPORTER ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15809054; DOI=10.1016/j.bbrc.2005.03.037;
RA Goytain A., Quamme G.A.;
RT "Functional characterization of the mouse solute carrier, SLC41A2.";
RL Biochem. Biophys. Res. Commun. 330:701-705(2005).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137 AND SER-138, AND
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: Acts as a plasma-membrane magnesium transporter
CC (PubMed:15809054). Can also mediate the transport of other divalent
CC metal cations in an order of Ba(2+) > Ni(2+) > Co(2+) > Fe(2+) > Mn(2+)
CC (PubMed:15809054). {ECO:0000269|PubMed:15809054}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Mg(2+)(in) = Mg(2+)(out); Xref=Rhea:RHEA:29827,
CC ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:15809054};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Mn(2+)(in) = Mn(2+)(out); Xref=Rhea:RHEA:28699,
CC ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:15809054};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Co(2+)(in) = Co(2+)(out); Xref=Rhea:RHEA:28578,
CC ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:15809054};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Ni(2+)(in) = Ni(2+)(out); Xref=Rhea:RHEA:29831,
CC ChEBI:CHEBI:49786; Evidence={ECO:0000269|PubMed:15809054};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Fe(2+)(in) = Fe(2+)(out); Xref=Rhea:RHEA:28486,
CC ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:15809054};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.34 mM for Mg(2+) {ECO:0000269|PubMed:15809054};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q96JW4};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the SLC41A transporter family. {ECO:0000305}.
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DR EMBL; AK038549; BAC30038.1; -; mRNA.
DR CCDS; CCDS24075.1; -.
DR RefSeq; NP_796362.1; NM_177388.3.
DR RefSeq; XP_006513874.1; XM_006513811.3.
DR RefSeq; XP_011241800.1; XM_011243498.2.
DR AlphaFoldDB; Q8BYR8; -.
DR STRING; 10090.ENSMUSP00000036690; -.
DR iPTMnet; Q8BYR8; -.
DR PhosphoSitePlus; Q8BYR8; -.
DR MaxQB; Q8BYR8; -.
DR PaxDb; 10090-ENSMUSP00000036690; -.
DR ProteomicsDB; 256904; -.
DR Antibodypedia; 30606; 169 antibodies from 17 providers.
DR DNASU; 338365; -.
DR Ensembl; ENSMUST00000039956.6; ENSMUSP00000036690.6; ENSMUSG00000034591.6.
DR GeneID; 338365; -.
DR KEGG; mmu:338365; -.
DR UCSC; uc007gkf.1; mouse.
DR AGR; MGI:2442940; -.
DR CTD; 84102; -.
DR MGI; MGI:2442940; Slc41a2.
DR VEuPathDB; HostDB:ENSMUSG00000034591; -.
DR eggNOG; KOG3788; Eukaryota.
DR GeneTree; ENSGT00950000183042; -.
DR HOGENOM; CLU_018207_3_0_1; -.
DR InParanoid; Q8BYR8; -.
DR OMA; HMDYHHF; -.
DR OrthoDB; 5124745at2759; -.
DR PhylomeDB; Q8BYR8; -.
DR TreeFam; TF313647; -.
DR Reactome; R-MMU-425410; Metal ion SLC transporters.
DR BioGRID-ORCS; 338365; 2 hits in 79 CRISPR screens.
DR ChiTaRS; Slc41a2; mouse.
DR PRO; PR:Q8BYR8; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8BYR8; Protein.
DR Bgee; ENSMUSG00000034591; Expressed in lacrimal gland and 190 other cell types or tissues.
DR ExpressionAtlas; Q8BYR8; baseline and differential.
DR Genevisible; Q8BYR8; MM.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0022890; F:inorganic cation transmembrane transporter activity; IDA:MGI.
DR GO; GO:0008324; F:monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006824; P:cobalt ion transport; IDA:UniProtKB.
DR GO; GO:0006826; P:iron ion transport; IDA:UniProtKB.
DR GO; GO:0015693; P:magnesium ion transport; IDA:UniProtKB.
DR GO; GO:0006828; P:manganese ion transport; IDA:UniProtKB.
DR GO; GO:0030001; P:metal ion transport; IDA:MGI.
DR GO; GO:0015675; P:nickel cation transport; IDA:UniProtKB.
DR Gene3D; 1.10.357.20; SLC41 divalent cation transporters, integral membrane domain; 2.
DR InterPro; IPR006667; SLC41_membr_dom.
DR InterPro; IPR036739; SLC41_membr_dom_sf.
DR InterPro; IPR045349; SLC41A1-3.
DR PANTHER; PTHR16228; DIVALENT CATION TRANSPORTER SOLUTE CARRIER FAMILY 41; 1.
DR PANTHER; PTHR16228:SF25; SOLUTE CARRIER FAMILY 41 MEMBER 2; 1.
DR Pfam; PF01769; MgtE; 2.
DR SUPFAM; SSF161093; MgtE membrane domain-like; 2.
PE 1: Evidence at protein level;
KW Cell membrane; Ion transport; Magnesium; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..573
FT /note="Solute carrier family 41 member 2"
FT /id="PRO_0000295042"
FT TOPO_DOM 1..162
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..195
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96JW4"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..245
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q96JW4"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..282
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96JW4"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..313
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q96JW4"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 335..347
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96JW4"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369..376
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q96JW4"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..406
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96JW4"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..469
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q96JW4"
FT TRANSMEM 470..490
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 491..498
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96JW4"
FT TRANSMEM 499..519
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 520..543
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q96JW4"
FT TRANSMEM 544..564
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 565..573
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96JW4"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 573 AA; 62305 MW; B4EAE989C4309B9E CRC64;
MTHSKGRPVT YKTSASPESG GGFVDWTLNL NTIQSDKFLN LLLSMVPVIY QKNQEDRHKK
VNGIWQDGLS GAAQTFSKRS EPHLDYHEFS EQAFHSSSSG HTPASCSPKY DDYAGYNYCD
GREASETTAM LQDEDLSSEG DDVIVETSQR IPKESSGVMA LQILVPFLLA GFGTVSAGMV
LDIVQHWEVF KNVTEVFILV PALLGLKGNL EMTLASRLST AVNVGKMDSP IEKWNLIIGN
LALKQVQATV VGFLAAVAAI ILGWIPEGKY YLSHSILLCS SSVATAFIAS LLQGIIMVGV
IVGSKKTGIN PDNVATPIAA SFGDLITLAI LAWISQGLYS CLETYYYISP LVCAFFLALT
PIWIIIAAKH PATRTVLHSG WEPVITAMVI SSIGGLILDT TVSDPNLVGI VVYTPVINGI
GGNLVAIQAS RISTYLHLHS IPGELPEEPK GCSYPFRTFF GSGVNNKSAQ VLLLFVIPGH
LIFLYTIHLM KSGHTSLTVV FVVVYLFAAV LQVFTLLWIA DWMVHRFWRK GKDPDSFSIP
YLTALGDLLG TALLALSFHF LWLIGDRDGD VGD
//
