MAL_MOUSE
ID MAL_MOUSE Reviewed; 153 AA.
AC O09198; O08819; O09109; Q545Q7; Q9D2R2;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Myelin and lymphocyte protein;
DE AltName: Full=T-lymphocyte maturation-associated protein;
GN Name=Mal;
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 / MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=9168137; DOI=10.1016/s0378-1119(96)00861-x;
RA Magyar J.P., Ebensperger C., Schaeren-Wiemers N., Suter U.;
RT "Myelin and lymphocyte protein (MAL/MVP17/VIP17) and plasmolipin are
RT members of an extended gene family.";
RL Gene 189:269-275(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION.
RX PubMed=9126323; DOI=10.1006/bbrc.1997.6338;
RA Perez P., Puertollano R., Alonso M.A.;
RT "Structural and biochemical similarities reveal a family of proteins
RT related to the MAL proteolipid, a component of detergent-insoluble membrane
RT microdomains.";
RL Biochem. Biophys. Res. Commun. 232:618-621(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Lung, Stomach, and Visual cortex;
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 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 [5]
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 [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15337780; DOI=10.1083/jcb.200406092;
RA Schaeren-Wiemers N., Bonnet A., Erb M., Erne B., Bartsch U., Kern F.,
RA Mantei N., Sherman D., Suter U.;
RT "The raft-associated protein MAL is required for maintenance of proper
RT axon-glia interactions in the central nervous system.";
RL J. Cell Biol. 166:731-742(2004).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=15193296; DOI=10.1016/j.nbd.2004.03.008;
RA Saravanan K., Schaeren-Wiemers N., Klein D., Sandhoff R., Schwarz A.,
RA Yaghootfam A., Gieselmann V., Franken S.;
RT "Specific downregulation and mistargeting of the lipid raft-associated
RT protein MAL in a glycolipid storage disorder.";
RL Neurobiol. Dis. 16:396-406(2004).
CC -!- FUNCTION: Could be an important component in vesicular trafficking
CC cycling between the Golgi complex and the apical plasma membrane. Plays
CC a role in the maintenance of the myelin sheath and in axon-glia and
CC glia-glia interactions. {ECO:0000269|PubMed:15337780}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane
CC protein. Apical cell membrane; Multi-pass membrane protein. Note=Found
CC in lipid raft.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=A;
CC IsoId=O09198-1; Sequence=Displayed;
CC Name=2; Synonyms=C;
CC IsoId=O09198-2; Sequence=VSP_031253;
CC -!- TISSUE SPECIFICITY: Expressed in the spinal cord, brain, kidney and
CC gastrointestinal tract especially in the stomach and caecum. Highly
CC expressed by myelinating glial cells. {ECO:0000269|PubMed:15337780}.
CC -!- PTM: Lipoprotein. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Abnormal myelination and optic nerve morphology.
CC {ECO:0000269|PubMed:15337780}.
CC -!- SIMILARITY: Belongs to the MAL family. {ECO:0000305}.
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DR EMBL; Y07626; CAA68907.1; -; mRNA.
DR EMBL; Y07627; CAA68908.1; -; Genomic_DNA.
DR EMBL; Y07628; CAA68908.1; JOINED; Genomic_DNA.
DR EMBL; Y07629; CAA68908.1; JOINED; Genomic_DNA.
DR EMBL; Y07630; CAA68908.1; JOINED; Genomic_DNA.
DR EMBL; Y07812; CAA69143.1; -; mRNA.
DR EMBL; AK004639; BAB23430.1; -; mRNA.
DR EMBL; AK019046; BAB31523.1; -; mRNA.
DR EMBL; AK158653; BAE34599.1; -; mRNA.
DR EMBL; AK169172; BAE40951.1; -; mRNA.
DR EMBL; AL731831; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL844204; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006826; AAH06826.1; -; mRNA.
DR CCDS; CCDS16707.1; -. [O09198-1]
DR CCDS; CCDS50705.1; -. [O09198-2]
DR RefSeq; NP_001164658.1; NM_001171187.1. [O09198-2]
DR RefSeq; NP_034892.1; NM_010762.5. [O09198-1]
DR AlphaFoldDB; O09198; -.
DR STRING; 10090.ENSMUSP00000028854; -.
DR PaxDb; O09198; -.
DR PRIDE; O09198; -.
DR Antibodypedia; 32290; 235 antibodies from 30 providers.
DR DNASU; 17153; -.
DR Ensembl; ENSMUST00000028853; ENSMUSP00000028853; ENSMUSG00000027375. [O09198-2]
DR Ensembl; ENSMUST00000028854; ENSMUSP00000028854; ENSMUSG00000027375. [O09198-1]
DR GeneID; 17153; -.
DR KEGG; mmu:17153; -.
DR UCSC; uc008mfv.2; mouse. [O09198-1]
DR UCSC; uc008mfw.2; mouse. [O09198-2]
DR CTD; 4118; -.
DR MGI; MGI:892970; Mal.
DR VEuPathDB; HostDB:ENSMUSG00000027375; -.
DR eggNOG; KOG4788; Eukaryota.
DR GeneTree; ENSGT00940000154987; -.
DR HOGENOM; CLU_112950_0_0_1; -.
DR InParanoid; O09198; -.
DR OMA; FPDIFFI; -.
DR OrthoDB; 1518300at2759; -.
DR PhylomeDB; O09198; -.
DR TreeFam; TF316174; -.
DR BioGRID-ORCS; 17153; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Mal; mouse.
DR PRO; PR:O09198; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; O09198; protein.
DR Bgee; ENSMUSG00000027375; Expressed in urinary bladder urothelium and 205 other tissues.
DR Genevisible; O09198; MM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0019898; C:extrinsic component of membrane; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0120003; C:hinge region between urothelial plaques of apical plasma membrane; IMP:MGI.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; IDA:MGI.
DR GO; GO:0044853; C:plasma membrane raft; IMP:MGI.
DR GO; GO:0019911; F:structural constituent of myelin sheath; ISO:MGI.
DR GO; GO:0022010; P:central nervous system myelination; IMP:MGI.
DR GO; GO:0042552; P:myelination; IMP:MGI.
DR GO; GO:1902043; P:positive regulation of extrinsic apoptotic signaling pathway via death domain receptors; IDA:MGI.
DR GO; GO:0098737; P:protein insertion into plasma membrane; IMP:MGI.
DR GO; GO:0002175; P:protein localization to paranode region of axon; IMP:MGI.
DR InterPro; IPR013295; MAL.
DR InterPro; IPR008253; Marvel.
DR Pfam; PF01284; MARVEL; 1.
DR PRINTS; PR01884; MALPROTEIN.
DR PROSITE; PS51225; MARVEL; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Golgi apparatus; Lipoprotein;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..153
FT /note="Myelin and lymphocyte protein"
FT /id="PRO_0000156806"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..53
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..125
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 18..151
FT /note="MARVEL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00581"
FT VAR_SEQ 32..87
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031253"
SQ SEQUENCE 153 AA; 16596 MW; 5EED415344669B4B CRC64;
MAPAAASGGS TLPSGFSVFT TFPDLLFVCE FVFGGLVWIL IASSLVPLPL AQGWVMFVSV
FCFVATTSLM ILYIIGTHGG ETSWITLDAA YHCVAALFYL SASVLEALAT ISMFDGFTYK
HYHENIAAVV FAYVVTLIYV VHAVFSLIRW KSS
