MLC1_MOUSE
ID MLC1_MOUSE Reviewed; 382 AA.
AC Q8VHK5;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Membrane protein MLC1;
GN Name=Mlc1;
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 [MRNA].
RC STRAIN=BALB/cJ;
RA Steinke V., Meyer J., Syagailo Y.V., Ortega G., Moessner R., Schmitt A.,
RA Lesch K.P.;
RT "The genomic organization of the murine Kiaa0027 (Wkl1, Mlc1) gene.";
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pituitary;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; SER-185 AND SER-188, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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: Regulates the response of astrocytes to hypo-osmosis by
CC promoting calcium influx. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ATP1B1. Part of a complex containing ATP1B1,
CC TRPV4, AQP4 and HEPACAM. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Cell membrane {ECO:0000250}. Cytoplasm,
CC perinuclear region {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}.
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DR EMBL; AF449425; AAL66020.1; -; mRNA.
DR EMBL; AK030396; BAC26941.1; -; mRNA.
DR EMBL; BC024719; AAH24719.1; -; mRNA.
DR CCDS; CCDS37173.1; -.
DR RefSeq; NP_573504.1; NM_133241.2.
DR AlphaFoldDB; Q8VHK5; -.
DR BioGRID; 228441; 2.
DR IntAct; Q8VHK5; 1.
DR MINT; Q8VHK5; -.
DR STRING; 10090.ENSMUSP00000047667; -.
DR iPTMnet; Q8VHK5; -.
DR PhosphoSitePlus; Q8VHK5; -.
DR SwissPalm; Q8VHK5; -.
DR MaxQB; Q8VHK5; -.
DR PaxDb; Q8VHK5; -.
DR PRIDE; Q8VHK5; -.
DR ProteomicsDB; 295680; -.
DR Antibodypedia; 297; 172 antibodies from 28 providers.
DR DNASU; 170790; -.
DR Ensembl; ENSMUST00000042594; ENSMUSP00000047667; ENSMUSG00000035805.
DR GeneID; 170790; -.
DR KEGG; mmu:170790; -.
DR UCSC; uc007xev.1; mouse.
DR CTD; 23209; -.
DR MGI; MGI:2157910; Mlc1.
DR VEuPathDB; HostDB:ENSMUSG00000035805; -.
DR eggNOG; ENOG502QUF1; Eukaryota.
DR GeneTree; ENSGT00390000015442; -.
DR HOGENOM; CLU_062641_0_0_1; -.
DR InParanoid; Q8VHK5; -.
DR OrthoDB; 856594at2759; -.
DR PhylomeDB; Q8VHK5; -.
DR TreeFam; TF333109; -.
DR BioGRID-ORCS; 170790; 0 hits in 71 CRISPR screens.
DR PRO; PR:Q8VHK5; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8VHK5; protein.
DR Bgee; ENSMUSG00000035805; Expressed in cranial nerve II and 86 other tissues.
DR ExpressionAtlas; Q8VHK5; baseline and differential.
DR Genevisible; Q8VHK5; MM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0097450; C:astrocyte end-foot; IDA:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0005901; C:caveola; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0072584; P:caveolin-mediated endocytosis; ISO:MGI.
DR GO; GO:0071397; P:cellular response to cholesterol; ISO:MGI.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0032388; P:positive regulation of intracellular transport; ISO:MGI.
DR GO; GO:0015031; P:protein transport; ISO:MGI.
DR GO; GO:0047484; P:regulation of response to osmotic stress; ISO:MGI.
DR GO; GO:0016192; P:vesicle-mediated transport; ISO:MGI.
DR InterPro; IPR033280; Membrane_MLC1.
DR PANTHER; PTHR17597; PTHR17597; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Endoplasmic reticulum; Ion channel;
KW Ion transport; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..382
FT /note="Membrane protein MLC1"
FT /id="PRO_0000096498"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 382 AA; 41596 MW; 0F5573B1F89327E0 CRC64;
MTREGQFREE LGYDRMPTLE RGRQDAGRQD PGSYTPDSKP KDLQLSKRLP PCFSYKTWVF
SVLMGSCLLV TSGFSLYLGN VFPSEMDYLR CAAGSCIPSA IVSFAVGRRN VSAIPNFQIL
FVSTFAVTTT CLIWFGCKLI LNPSAININF NLILLLLLEL LMAATVIISA RSSEEPCKKK
KGSISDGSNI LDEVTFPARV LKSYSVVEVI AGVSAVLGGV IALNVEEAVS GPHLSVTFFW
ILVACFPSAI ASHVTAECPS KCLVEVLIAI SSLTSPLLFT ASGYLSFSVM RVVEIFKDYP
PAIKSYDVLL LLLLLLLLLQ GGLNTGTAIQ CVSFKVSARL QAASWDPQSC PQERPAGEVV
RGPLKEFDKE KAWRAVVVQM AQ
