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Database: UniProt
Entry: MIA2_MOUSE
LinkDB: MIA2_MOUSE
Original site: 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   08-NOV-2023, entry version 143.
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   BioGRID; 237201; 1.
DR   STRING; 10090.ENSMUSP00000070572; -.
DR   GlyCosmos; Q91ZV0; 2 sites, No reported glycans.
DR   GlyGen; Q91ZV0; 2 sites.
DR   iPTMnet; Q91ZV0; -.
DR   PhosphoSitePlus; Q91ZV0; -.
DR   SwissPalm; Q91ZV0; -.
DR   jPOST; Q91ZV0; -.
DR   MaxQB; Q91ZV0; -.
DR   PaxDb; 10090-ENSMUSP00000070572; -.
DR   PeptideAtlas; Q91ZV0; -.
DR   ProteomicsDB; 284142; -.
DR   ProteomicsDB; 295901; -. [Q91ZV0-1]
DR   ProteomicsDB; 295902; -. [Q91ZV0-2]
DR   Pumba; Q91ZV0; -.
DR   DNASU; 338320; -.
DR   UCSC; uc007nqc.1; mouse. [Q91ZV0-1]
DR   AGR; MGI:2159614; -.
DR   MGI; MGI:2159614; Mia2.
DR   eggNOG; ENOG502QUND; Eukaryota.
DR   HOGENOM; CLU_028032_0_0_1; -.
DR   InParanoid; Q91ZV0; -.
DR   TreeFam; TF332724; -.
DR   Reactome; R-MMU-5694530; Cargo concentration in the ER.
DR   BioGRID-ORCS; 338320; 12 hits in 81 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: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   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR23158:SF38; MELANOMA INHIBITORY ACTIVITY PROTEIN 2; 1.
DR   PANTHER; PTHR23158; MELANOMA INHIBITORY ACTIVITY-RELATED; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   SUPFAM; SSF50044; SH3-domain; 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
//
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