MBRL_MOUSE
ID MBRL_MOUSE Reviewed; 574 AA.
AC Q8CIV2; Q68EE1; Q6KAN7; Q7TS84; Q8CIV1; Q99K29;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Membralin;
DE AltName: Full=Transmembrane protein 259;
GN Name=Tmem259; Synonyms=ORF61;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RX PubMed=12638133; DOI=10.1016/s1567-133x(02)00019-4;
RA Andersson O., von Euler G.;
RT "Characterization and expression of the gene encoding membralin, an
RT evolutionary conserved protein expressed in the central nervous system.";
RL Gene Expr. Patterns 1:205-212(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 91-574 (ISOFORM 1).
RC TISSUE=Mammary gland;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 374-574.
RC TISSUE=Embryonic tail;
RX PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of FLJ genes: the
RT complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified
RT by screening of terminal sequences of cDNA clones randomly sampled from
RT size-fractionated libraries.";
RL DNA Res. 11:127-135(2004).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-180.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, and Lung;
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).
RN [6]
RP FUNCTION, INTERACTION WITH ERLIN2, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=25977983; DOI=10.7554/elife.06500;
RA Yang B., Qu M., Wang R., Chatterton J.E., Liu X.B., Zhu B., Narisawa S.,
RA Millan J.L., Nakanishi N., Swoboda K., Lipton S.A., Zhang D.;
RT "The critical role of membralin in postnatal motor neuron survival and
RT disease.";
RL Elife 4:0-0(2015).
CC -!- FUNCTION: May have a role in the ERAD pathway required for clearance of
CC misfolded proteins in the endoplasmic reticulum (ER). Promotes survival
CC of motor neurons, probably by protecting against ER stress.
CC {ECO:0000269|PubMed:25977983}.
CC -!- SUBUNIT: Interacts with ERLIN2. {ECO:0000269|PubMed:25977983}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:25977983}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Membralin-1;
CC IsoId=Q8CIV2-1; Sequence=Displayed;
CC Name=2; Synonyms=Membralin-2;
CC IsoId=Q8CIV2-2; Sequence=VSP_014379;
CC -!- TISSUE SPECIFICITY: Detected in brain, spinal cord, lung, liver and
CC kidney. {ECO:0000269|PubMed:25977983}.
CC -!- DISRUPTION PHENOTYPE: Lethality typically occurs several days after
CC birth, associated with motor neuron deficiency and paresis.
CC {ECO:0000269|PubMed:25977983}.
CC -!- SIMILARITY: Belongs to the membralin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH52787.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY096037; AAM34493.1; -; mRNA.
DR EMBL; AY096036; AAM34492.1; -; mRNA.
DR EMBL; BC005494; AAH05494.1; -; mRNA.
DR EMBL; BC052787; AAH52787.1; ALT_INIT; mRNA.
DR EMBL; AK131170; BAD21420.1; -; mRNA.
DR CCDS; CCDS24002.1; -. [Q8CIV2-1]
DR RefSeq; NP_001003949.2; NM_001003949.3. [Q8CIV2-1]
DR RefSeq; XP_006513553.1; XM_006513490.1.
DR AlphaFoldDB; Q8CIV2; -.
DR BioGRID; 229711; 2.
DR IntAct; Q8CIV2; 1.
DR STRING; 10090.ENSMUSP00000056792; -.
DR GlyConnect; 2506; 5 N-Linked glycans (1 site).
DR GlyGen; Q8CIV2; 1 site, 5 N-linked glycans (1 site).
DR iPTMnet; Q8CIV2; -.
DR PhosphoSitePlus; Q8CIV2; -.
DR EPD; Q8CIV2; -.
DR MaxQB; Q8CIV2; -.
DR PaxDb; Q8CIV2; -.
DR PeptideAtlas; Q8CIV2; -.
DR PRIDE; Q8CIV2; -.
DR ProteomicsDB; 295973; -. [Q8CIV2-1]
DR ProteomicsDB; 295974; -. [Q8CIV2-2]
DR Antibodypedia; 10308; 76 antibodies from 18 providers.
DR DNASU; 216157; -.
DR Ensembl; ENSMUST00000052885; ENSMUSP00000056792; ENSMUSG00000013858. [Q8CIV2-1]
DR GeneID; 216157; -.
DR KEGG; mmu:216157; -.
DR UCSC; uc007gax.1; mouse. [Q8CIV2-1]
DR UCSC; uc007gay.1; mouse. [Q8CIV2-2]
DR CTD; 91304; -.
DR MGI; MGI:2177957; Tmem259.
DR VEuPathDB; HostDB:ENSMUSG00000013858; -.
DR eggNOG; KOG2092; Eukaryota.
DR GeneTree; ENSGT00390000013329; -.
DR InParanoid; Q8CIV2; -.
DR OMA; MTVDMFE; -.
DR OrthoDB; 426985at2759; -.
DR PhylomeDB; Q8CIV2; -.
DR TreeFam; TF313323; -.
DR BioGRID-ORCS; 216157; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Tmem259; mouse.
DR PRO; PR:Q8CIV2; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8CIV2; protein.
DR Bgee; ENSMUSG00000013858; Expressed in ankle joint and 251 other tissues.
DR ExpressionAtlas; Q8CIV2; baseline and differential.
DR Genevisible; Q8CIV2; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:1901215; P:negative regulation of neuron death; IMP:UniProtKB.
DR GO; GO:1904294; P:positive regulation of ERAD pathway; IDA:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:UniProtKB.
DR InterPro; IPR019144; Membralin.
DR PANTHER; PTHR21650:SF4; PTHR21650:SF4; 1.
DR Pfam; PF09746; Membralin; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Endoplasmic reticulum; Glycoprotein;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q4ZIN3"
FT CHAIN 2..574
FT /note="Membralin"
FT /id="PRO_0000096274"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q4ZIN3"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT VAR_SEQ 324
FT /note="I -> IGESQPAGGGVGSPQALMGGRPVPA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12638133"
FT /id="VSP_014379"
FT CONFLICT 83
FT /note="A -> V (in Ref. 1; AAM34493)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="N -> D (in Ref. 1; AAM34492)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="D -> V (in Ref. 1; AAM34492)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="P -> S (in Ref. 1; AAM34493)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="E -> G (in Ref. 1; AAM34493)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="I -> F (in Ref. 1; AAM34493)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="F -> S (in Ref. 1; AAM34492)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="M -> V (in Ref. 1; AAM34493)"
FT /evidence="ECO:0000305"
FT CONFLICT 374..396
FT /note="TVWLADQYDAICCHTNTSKRHWL -> GASWAPGWDREGPVWQGSFSRPH
FT (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 423
FT /note="V -> D (in Ref. 1; AAM34493)"
FT /evidence="ECO:0000305"
FT CONFLICT 540
FT /note="S -> N (in Ref. 1; AAM34493)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 574 AA; 63561 MW; 898C0EBDF9B25FD1 CRC64;
MSEHAAAPGP GPNGGGGGGA APVRGPRGPN LNPNPLINVR DRLFHALFFK MAVTYSRLFP
PAFRRLFEFF VLLKALFVLF VLAYIHIVFS RSPINCLEHV RDRWPREGVL RVEVRHNSSR
APVILQFCDG GLGGLELEPG GLELEEEELT VEMFTNSSIK FELDIEPKVF KPQSGADALN
DSQDFPFPET PAKVWPQDEY IVEYSLEYGF LRLSQATRQR LSIPVMVVTL DPTRDQCFGD
RFSRLLLDEF LGYDDILMSS VKGLAENEEN KGFLRNVVSG EHYRFVSMWM ARTSYLAAFV
IMVIFTLSVS MLLRYSHHQI FVFIVDLLQM LEMNMAIAFP AAPLLTVILA LVGMEAIMSE
FFNDTTTAFY IILTVWLADQ YDAICCHTNT SKRHWLRFFY LYHFAFYAYH YRFNGQYSSL
ALVTSWLFIQ HSMIYFFHHY ELPAILQQIR IQEMLLQTPP LGPGTPTALP DDLNNNSGSP
ATPDPSPPLA LGPSSSPAPT GGASGPGSLG AGASVSGSDL GWVAETAAII SDASFLSGLS
ASLLERRPTA PSTPDSSRPD PGVPLEDAPA PAGS
