MIA2_MOUSE
ID MIA2_MOUSE Reviewed; 1396 AA.
AC Q91ZV0; Q8CIE3; Q8R311;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-SEP-2016, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Melanoma inhibitory activity protein 2 {ECO:0000305};
DE AltName: Full=CTAGE family member 5 ER export factor {ECO:0000250|UniProtKB:Q96PC5};
DE Flags: Precursor;
GN Name=Mia2 {ECO:0000312|MGI:MGI:2159614};
GN Synonyms=Ctage5 {ECO:0000250|UniProtKB:Q96PC5};
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] (ISOFORM 2), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=12586826; DOI=10.1074/jbc.m212639200;
RA Bosserhoff A.K., Moser M., Schoelmerich J., Buettner R., Hellerbrand C.;
RT "Specific expression and regulation of the new melanoma inhibitory
RT activity-related gene MIA2 in hepatocytes.";
RL J. Biol. Chem. 278:15225-15231(2003).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, and Pancreas;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=FVB/N; TISSUE=Liver, and 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 [4]
RP FUNCTION, INTERACTION WITH SEC23A AND SEC24C, SUBCELLULAR LOCATION,
RP TOPOLOGY, TISSUE SPECIFICITY, DOMAIN, REGION, AND MUTAGENESIS OF PHE-90.
RX PubMed=21807889; DOI=10.1194/jlr.m017277;
RA Pitman J.L., Bonnet D.J., Curtiss L.K., Gekakis N.;
RT "Reduced cholesterol and triglycerides in mice with a mutation in Mia2, a
RT liver protein that localizes to ER exit sites.";
RL J. Lipid Res. 52:1775-1786(2011).
CC -!- FUNCTION: Plays a role in the transport of cargos that are too large to
CC fit into COPII-coated vesicles and require specific mechanisms to be
CC incorporated into membrane-bound carriers and exported from the
CC endoplasmic reticulum. Plays a role in the secretion of lipoproteins,
CC pre-chylomicrons and pre-VLDLs, by participating in their export from
CC the endoplasmic reticulum (By similarity). Thereby, may play a role in
CC cholesterol and triglyceride homeostasis (PubMed:21807889). Required
CC for collagen VII (COL7A1) secretion by loading COL7A1 into transport
CC carriers and recruiting PREB/SEC12 at the endoplasmic reticulum exit
CC sites (By similarity). {ECO:0000250|UniProtKB:Q96PC5,
CC ECO:0000269|PubMed:21807889}.
CC -!- SUBUNIT: Interacts with MIA3 (By similarity). Interacts with the COPII
CC coat subunits SEC23A, SEC23B and maybe SEC24C (By similarity)
CC (PubMed:21807889). Interacts with PREB; recruits PREB to endoplasmic
CC reticulum exit sites. Interacts with APOB (By similarity).
CC {ECO:0000250|UniProtKB:Q96PC5, ECO:0000269|PubMed:21807889}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21807889}; Single-pass membrane protein
CC {ECO:0000305|PubMed:21807889}. Note=Localizes to endoplasmic reticulum
CC exit sites (ERES), also known as transitional endoplasmic reticulum
CC (tER). {ECO:0000269|PubMed:21807889}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Mia2 p240 {ECO:0000303|PubMed:21807889};
CC IsoId=Q91ZV0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91ZV0-2; Sequence=VSP_058474, VSP_058475;
CC Name=3;
CC IsoId=Q91ZV0-3; Sequence=VSP_060016;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in liver (at protein level)
CC (PubMed:12586826, PubMed:21807889). Isoform 2 is highly expressed in
CC liver and weakly in testis (PubMed:12586826).
CC {ECO:0000269|PubMed:12586826, ECO:0000269|PubMed:21807889}.
CC -!- DEVELOPMENTAL STAGE: Expression is seen at 12.5 dpc and 14.5 dpc
CC embryonic stages. {ECO:0000269|PubMed:12586826}.
CC -!- DOMAIN: The proline-rich domain (PRD) contains repeated PPP motifs. A
CC single PPP motif is necessary and sufficient to mediate interaction
CC with the COPII coat subunits SEC23A and SEC23B (PubMed:21807889). The
CC coiled coil domains mediate interaction with MIA3. The first coiled
CC coil domain mediates interaction with PREB (By similarity).
CC {ECO:0000250|UniProtKB:Q96PC5, ECO:0000269|PubMed:21807889}.
CC -!- MISCELLANEOUS: [Isoform 1]: Readthrough transcript producing a
CC functional fusion protein MIA2-CTAGE5 with similarity to MIA3.
CC {ECO:0000305|PubMed:21807889}.
CC -!- SIMILARITY: Belongs to the MIA/OTOR family. {ECO:0000305}.
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DR EMBL; AF390177; AAL26992.2; -; mRNA.
DR EMBL; BC024076; AAH24076.1; -; mRNA.
DR EMBL; BC026864; AAH26864.1; -; mRNA.
DR RefSeq; NP_796295.1; NM_177321.2.
DR AlphaFoldDB; Q91ZV0; -.
DR SMR; Q91ZV0; -.
DR STRING; 10090.ENSMUSP00000070572; -.
DR GlyGen; Q91ZV0; 2 sites.
DR iPTMnet; Q91ZV0; -.
DR PhosphoSitePlus; Q91ZV0; -.
DR jPOST; Q91ZV0; -.
DR MaxQB; Q91ZV0; -.
DR PaxDb; Q91ZV0; -.
DR PeptideAtlas; Q91ZV0; -.
DR PRIDE; Q91ZV0; -.
DR ProteomicsDB; 284142; -.
DR ProteomicsDB; 295901; -. [Q91ZV0-1]
DR ProteomicsDB; 295902; -. [Q91ZV0-2]
DR DNASU; 338320; -.
DR UCSC; uc007nqc.1; mouse. [Q91ZV0-1]
DR MGI; MGI:2159614; Mia2.
DR eggNOG; ENOG502QUND; Eukaryota.
DR HOGENOM; CLU_028032_0_0_1; -.
DR InParanoid; Q91ZV0; -.
DR OrthoDB; 310143at2759; -.
DR TreeFam; TF332724; -.
DR Reactome; R-MMU-5694530; Cargo concentration in the ER.
DR BioGRID-ORCS; 338320; 11 hits in 76 CRISPR screens.
DR ChiTaRS; Mia2; mouse.
DR PRO; PR:Q91ZV0; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q91ZV0; protein.
DR Genevisible; Q91ZV0; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0038024; F:cargo receptor activity; ISS:UniProtKB.
DR GO; GO:0042632; P:cholesterol homeostasis; IMP:MGI.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:UniProtKB.
DR GO; GO:0042953; P:lipoprotein transport; ISS:UniProtKB.
DR GO; GO:0032527; P:protein exit from endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0070973; P:protein localization to endoplasmic reticulum exit site; ISS:UniProtKB.
DR GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR GO; GO:0070328; P:triglyceride homeostasis; IMP:MGI.
DR GO; GO:0035459; P:vesicle cargo loading; ISS:UniProtKB.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF07653; SH3_2; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Endoplasmic reticulum; Glycoprotein;
KW Membrane; Reference proteome; SH3 domain; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1396
FT /note="Melanoma inhibitory activity protein 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000019032"
FT TOPO_DOM 23..604
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT INTRAMEM 605..625
FT /evidence="ECO:0000255"
FT TOPO_DOM 626..628
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 629..649
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 650..1396
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 39..101
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 197..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..1243
FT /note="Mediates interaction with MIA3"
FT /evidence="ECO:0000250|UniProtKB:Q96PC5"
FT REGION 1103..1396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1105..1396
FT /note="Proline-rich domain (PRD); probably mediates
FT interaction with COPII coat subunits"
FT /evidence="ECO:0000269|PubMed:21807889"
FT COILED 693..867
FT /evidence="ECO:0000255"
FT COILED 914..1082
FT /evidence="ECO:0000255"
FT COMPBIAS 231..245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..548
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1162..1182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1252..1269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1308..1388
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..619
FT /note="Missing (in isoform 3)"
FT /id="VSP_060016"
FT VAR_SEQ 517
FT /note="D -> G (in isoform 2)"
FT /id="VSP_058474"
FT VAR_SEQ 518..1396
FT /note="Missing (in isoform 2)"
FT /id="VSP_058475"
FT MUTAGEN 90
FT /note="F->S: Decreases expression of isoform 1."
FT /evidence="ECO:0000269|PubMed:21807889"
FT CONFLICT 880
FT /note="E -> EDI (in Ref. 3; AAH24076/AAH26864)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1396 AA; 156461 MW; 152ED0302432C438 CRC64;
MAEVSVQRIL LLVVSLAKCL EGTKLLAHLK KCGDLECETL ISRVLALRDY TGPDCRYLNF
TTGEEISVYV KLGGDREDLW AGSKGKDFGF FPRDAVEIEE VFISEEVEMP TKSDFLCLLG
EGYIFGSEQS ELNSEDDEEH MYPYEKDEDQ NYNIYEGDFQ PEPDLYAAAE GTLLEDQIPA
SEAPDDFRFS SEWKAWEGAG SQGGGEQDYT ADSDQDLPSL SKPERQGWFG LGTEEAEEKV
FESDTEPTQE LALEEESDLE KLHSGEPQVE LEQEPKSETL EFSSVPDEEY ELESETESIL
KPQASGWFGE GLTSYLGFGN EEAGLELLSK ESNPPLQDIP SSVPPDEEVP APCREISTDK
EDAVINDSSV LSPSWFYYGF GMLGFTNADE DNIVSDKGEN EDGEVDNLKH PIGSDFDPEK
EQERKIVTVE TEDQAGTESV LEKTDESGSM QYLKKFFDNP WGFQSLPEDT ELPFSKKMLD
QDDIVENDKI EELSTENSPT GSMKDPVMLA SRYVLSDIDS EVELPMEEHE GVHFKPSSSK
RNEDDSNSWA DPEELSVAQT DGSAEGALLD TQLVSPKEHA ADFQLLKYLL QIDVYGFMSS
ALSPIEILLE SVVAALPEDM RADFNPSGFS LELAVCVLSV GLLAVVLFLW RGFRSIRSRF
YVGREKKLAL ELSALIEEKC KLLDKVSIVQ KEYEGLESSL KEASFEKEST EAQSLEFVEG
SQISEATYEN LEQSKSKLED EILLLEEKLE EERAKHSEQD ELMADISKRI QSLEDESKSL
KSQVAEAKTT FRIFEINEER LKGAIKDALN ENSQLQESQK QLLQETEMMK EQVNDLDKQK
VALEESRAQA EQALSEKESQ IETLVTSLLK MKDWAAVLGE ADDGNLDLDM KSGLENTAAL
DNQPKGALKK LIYAAKLNAS LKALEGERNQ VYTQLSEVDQ VKEDLTEHIK SLESKQASLQ
SEKTEFESES QKLQQKLKVI TELYQENEMK LHRKLTVEEN YRLEKEEKLS KVDEKISHAT
EELETCRQRA KDLEEELERT IHSYQGQVIS HEKKAHDNWL AARTLERNLN DLRKENAHNR
QKLTETEFKF ELLEKDPYAL DVPNTAFGRE HSPYGPSPLG RPPSETRAFL SPPTLLEGPL
RLSPLLPGGG GRGSRGPENL LDHQMNTERG ESSYDRLSDA PRAPSDRSLS PPWEQDRRMT
AHPPPGQPYS DPALQRQDRF YPNSGRLSGP AELRSYNMPS LDKVDGPVPS EMESSGNGTK
DNLGNSNVPD SPIPAECEAA GRGFFPPPFP PVRDPLFPVD PRSQFMRRGP SFPPPPPGSI
YAAPRDYFPP RDFPGPPLPP FPGRTVYAPR GFPPYLPPRA GFFPPPPHPE SRSELPPDLI
PPSKEPAADP PETQEA
