MIA2_HUMAN
ID MIA2_HUMAN Reviewed; 1412 AA.
AC Q96PC5; A0A193H6U5; A1L4H0; B3KRA6; B4DQS6; D3DSA6; G3XAC5; O00169; O15320;
AC Q6MZN2; Q6P2R8; Q86TF6; Q8IX92; Q8IX93; Q9H6C1;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-SEP-2016, sequence version 4.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Melanoma inhibitory activity protein 2 {ECO:0000305};
DE Short=MIA protein 2;
DE AltName: Full=CTAGE family member 5 ER export factor {ECO:0000312|HGNC:HGNC:18432};
DE AltName: Full=Cutaneous T-cell lymphoma-associated antigen 5;
DE AltName: Full=Meningioma-expressed antigen 6/11 {ECO:0000303|PubMed:9356211};
DE Flags: Precursor;
GN Name=MIA2 {ECO:0000312|HGNC:HGNC:18432};
GN Synonyms=CTAGE5 {ECO:0000312|HGNC:HGNC:18432}, MEA11, MEA6, MGEA11, MGEA6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6 AND 7), AND VARIANTS ALA-6 (ISOFORMS
RP 6 AND 7); GLN-968; VAL-1307 AND ARG-1346.
RC TISSUE=Meningioma;
RX PubMed=9356211; DOI=10.1093/hmg/6.12.2031;
RA Heckel D., Brass N., Fischer U., Blin N., Steudel I., Tuereci O.,
RA Fackler O., Zang K.D., Meese E.;
RT "cDNA cloning and chromosomal mapping of a predicted coiled-coil proline-
RT rich protein immunogenic in meningioma patients.";
RL Hum. Mol. Genet. 6:2031-2041(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 8 AND 9), VARIANT ALA-6 (ISOFORM 9),
RP VARIANTS GLN-968 AND ARG-1346, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=12839582; DOI=10.1046/j.1523-1747.2003.12318.x;
RA Usener D., Schadendorf D., Koch J., Duebel S., Eichmueller S.;
RT "cTAGE: a cutaneous T cell lymphoma associated antigen family with tumor-
RT specific splicing.";
RL J. Invest. Dermatol. 121:198-206(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH APOB AND
RP MIA3, AND TISSUE SPECIFICITY.
RX PubMed=27138255; DOI=10.1083/jcb.201603072;
RA Santos A.J., Nogueira C., Ortega-Bellido M., Malhotra V.;
RT "TANGO1 and Mia2/cTAGE5 (TALI) cooperate to export bulky pre-
RT chylomicrons/VLDLs from the endoplasmic reticulum.";
RL J. Cell Biol. 213:343-354(2016).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 200-1412 (ISOFORM 2), AND VARIANTS GLN-968
RP AND VAL-1307.
RC TISSUE=Teratocarcinoma, and Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 10), AND VARIANTS GLN-968
RP AND ARG-1346.
RC TISSUE=Salivary gland;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 11 AND 12), VARIANT
RP ASP-11 (ISOFORM 11), AND VARIANTS ASN-813 AND VAL-1307.
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 [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-522 (ISOFORM 1/2), AND TISSUE SPECIFICITY.
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 [10]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
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).
RN [11]
RP FUNCTION, INTERACTION WITH MIA3; SEC23A AND SEC24C, SUBCELLULAR LOCATION,
RP DOMAIN, AND REGION.
RX PubMed=21525241; DOI=10.1091/mbc.e11-02-0143;
RA Saito K., Yamashiro K., Ichikawa Y., Erlmann P., Kontani K., Malhotra V.,
RA Katada T.;
RT "cTAGE5 mediates collagen secretion through interaction with TANGO1 at
RT endoplasmic reticulum exit sites.";
RL Mol. Biol. Cell 22:2301-2308(2011).
RN [12]
RP FUNCTION, INTERACTION WITH MIA3 AND PREB, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=25202031; DOI=10.1083/jcb.201312062;
RA Saito K., Yamashiro K., Shimazu N., Tanabe T., Kontani K., Katada T.;
RT "Concentration of Sec12 at ER exit sites via interaction with cTAGE5 is
RT required for collagen export.";
RL J. Cell Biol. 206:751-762(2014).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP FUNCTION, INTERACTION WITH MIA3 AND PREB, AND MUTAGENESIS OF TYR-679;
RP LYS-697; SER-705 AND LEU-720.
RX PubMed=27170179; DOI=10.1091/mbc.e16-03-0180;
RA Tanabe T., Maeda M., Saito K., Katada T.;
RT "Dual function of cTAGE5 in collagen export from the endoplasmic
RT reticulum.";
RL Mol. Biol. Cell 27:2008-2013(2016).
RN [15]
RP INTERACTION WITH SEC23A AND SEC23B, DOMAIN, AND REGION.
RX PubMed=27551091; DOI=10.1073/pnas.1605916113;
RA Ma W., Goldberg J.;
RT "TANGO1/cTAGE5 receptor as a polyvalent template for assembly of large
RT COPII coats.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:10061-10066(2016).
RN [16]
RP SUBCELLULAR LOCATION.
RX PubMed=28442536; DOI=10.1083/jcb.201703084;
RA Maeda M., Katada T., Saito K.;
RT "TANGO1 recruits Sec16 to coordinately organize ER exit sites for efficient
RT secretion.";
RL J. Cell Biol. 216:1731-1743(2017).
RN [17]
RP VARIANT [LARGE SCALE ANALYSIS] HIS-437.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
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 (PubMed:27138255, PubMed:21525241,
CC PubMed:25202031, PubMed:27170179). Plays a role in the secretion of
CC lipoproteins, pre-chylomicrons and pre-VLDLs, by participating in their
CC export from the endoplasmic reticulum (PubMed:27138255). Thereby, may
CC play a role in cholesterol and triglyceride homeostasis (By
CC similarity). Required for collagen VII (COL7A1) secretion by loading
CC COL7A1 into transport carriers and recruiting PREB/SEC12 at the
CC endoplasmic reticulum exit sites (PubMed:21525241, PubMed:25202031,
CC PubMed:27170179). {ECO:0000250|UniProtKB:Q91ZV0,
CC ECO:0000269|PubMed:21525241, ECO:0000269|PubMed:25202031,
CC ECO:0000269|PubMed:27138255, ECO:0000269|PubMed:27170179}.
CC -!- SUBUNIT: Interacts with MIA3 (PubMed:21525241, PubMed:25202031,
CC PubMed:27138255, PubMed:27170179). Interacts with the COPII coat
CC subunits SEC23A, SEC23B and maybe SEC24C (PubMed:21525241,
CC PubMed:27551091). Interacts with PREB; recruits PREB to endoplasmic
CC reticulum exit sites (PubMed:25202031, PubMed:27170179). Interacts with
CC APOB (PubMed:27138255). {ECO:0000269|PubMed:21525241,
CC ECO:0000269|PubMed:25202031, ECO:0000269|PubMed:27138255,
CC ECO:0000269|PubMed:27170179, ECO:0000269|PubMed:27551091}.
CC -!- INTERACTION:
CC Q96PC5; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-1050253, EBI-10175300;
CC Q96PC5; Q86XR8: CEP57; NbExp=3; IntAct=EBI-1050253, EBI-308614;
CC Q96PC5; Q9Y6C2: EMILIN1; NbExp=3; IntAct=EBI-1050253, EBI-744586;
CC Q96PC5; Q96M61: MAGEB18; NbExp=3; IntAct=EBI-1050253, EBI-741835;
CC Q96PC5; P25788: PSMA3; NbExp=3; IntAct=EBI-1050253, EBI-348380;
CC Q96PC5; Q9UJF2: RASAL2; NbExp=3; IntAct=EBI-1050253, EBI-359444;
CC Q96PC5; O75177: SS18L1; NbExp=3; IntAct=EBI-1050253, EBI-744674;
CC Q96PC5; Q08117: TLE5; NbExp=3; IntAct=EBI-1050253, EBI-717810;
CC Q96PC5; Q6PF05-3: TTC23L; NbExp=3; IntAct=EBI-1050253, EBI-10182647;
CC Q96PC5; Q15326: ZMYND11; NbExp=2; IntAct=EBI-1050253, EBI-2623509;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21525241, ECO:0000269|PubMed:21807889,
CC ECO:0000269|PubMed:25202031, ECO:0000269|PubMed:28442536}; Single-pass
CC membrane protein {ECO:0000269|PubMed:21807889}. Note=Localizes to
CC endoplasmic reticulum exit sites (ERES), also known as transitional
CC endoplasmic reticulum (tER). {ECO:0000269|PubMed:21525241,
CC ECO:0000269|PubMed:21807889, ECO:0000269|PubMed:25202031,
CC ECO:0000269|PubMed:28442536}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=12;
CC Name=1; Synonyms=TALI {ECO:0000303|PubMed:27138255};
CC IsoId=Q96PC5-3; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96PC5-2; Sequence=VSP_058472, VSP_058473;
CC Name=4;
CC IsoId=Q96PC5-5; Sequence=VSP_060004, VSP_060011;
CC Name=5;
CC IsoId=Q96PC5-6; Sequence=VSP_060005, VSP_060008, VSP_060009,
CC VSP_060012, VSP_060013;
CC Name=6; Synonyms=MEA6;
CC IsoId=Q96PC5-7; Sequence=VSP_060006, VSP_060007;
CC Name=7; Synonyms=MEA11;
CC IsoId=Q96PC5-8; Sequence=VSP_060006, VSP_060007, VSP_060011;
CC Name=8; Synonyms=5A;
CC IsoId=Q96PC5-9; Sequence=VSP_060004;
CC Name=9; Synonyms=5B;
CC IsoId=Q96PC5-10; Sequence=VSP_060006, VSP_060007, VSP_060014,
CC VSP_060015;
CC Name=10;
CC IsoId=Q96PC5-11; Sequence=VSP_060003;
CC Name=11;
CC IsoId=Q96PC5-12; Sequence=VSP_060006, VSP_060007, VSP_060010;
CC Name=12;
CC IsoId=Q96PC5-13; Sequence=VSP_060003, VSP_060010;
CC Name=13;
CC IsoId=Q96PC5-14; Sequence=VSP_060005, VSP_060008;
CC -!- TISSUE SPECIFICITY: Highly expressed in liver and weakly in testis.
CC Expression was higher in patients with severe fibrosis or inflammation
CC and chronic hepatitis (PubMed:12586826). Isoform 1 is specifically
CC expressed in lung, testis, small intestine, colon, pancreas, kidney,
CC liver and prostate (PubMed:27138255). Isoform 8 is expressed only in
CC testis (at the protein level). Isoform 8 (at protein level) and isoform
CC 9 are expressed in cutaneous T-cell lymphoma (CTCL) cell lines,
CC colorectal carcinomas, breast carcinomas and melanoma. Isoform 9, but
CC not isoform 5A, is expressed in head and neck squamous cell carcinoma
CC (PubMed:12839582). {ECO:0000269|PubMed:12586826,
CC ECO:0000269|PubMed:12839582, ECO:0000269|PubMed:27138255}.
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:21525241,
CC PubMed:27551091). The coiled coil domains mediate interaction with MIA3
CC (PubMed:21525241). The first coiled coil domain mediates interaction
CC with PREB (PubMed:25202031). {ECO:0000269|PubMed:21525241,
CC ECO:0000269|PubMed:25202031, ECO:0000269|PubMed:27551091}.
CC -!- DISEASE: Note=Autoantibodies against MIA2 are present in several cancer
CC types, including benign meningioma and cutaneous T-cell lymphoma
CC (CTCL).
CC -!- MISCELLANEOUS: [Isoform 1]: Readthrough transcript producing a
CC functional fusion protein MIA2-CTAGE5 with similarity to MIA3.
CC {ECO:0000305|PubMed:21807889, ECO:0000305|PubMed:27138255}.
CC -!- SIMILARITY: Belongs to the MIA/OTOR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB86589.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAL26990.2; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=BAB15339.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U73682; AAB86589.1; ALT_INIT; mRNA.
DR EMBL; U94780; AAB86593.1; -; mRNA.
DR EMBL; AF338233; AAN77610.1; -; mRNA.
DR EMBL; AF338234; AAN77611.1; -; mRNA.
DR EMBL; KX388743; ANN89694.1; -; mRNA.
DR EMBL; AK026057; BAB15339.1; ALT_INIT; mRNA.
DR EMBL; AK091252; BAG52318.1; -; mRNA.
DR EMBL; AK298935; BAG61038.1; -; mRNA.
DR EMBL; BX640994; CAE45997.1; -; mRNA.
DR EMBL; AL132639; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL157791; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471078; EAW65808.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW65812.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW65813.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW65814.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW65818.1; -; Genomic_DNA.
DR EMBL; BC051363; AAH51363.2; -; mRNA.
DR EMBL; BC064355; AAH64355.1; -; mRNA.
DR EMBL; BC130537; AAI30538.1; -; mRNA.
DR EMBL; BC130563; AAI30564.1; -; mRNA.
DR EMBL; AF390175; AAL26990.2; ALT_SEQ; mRNA.
DR CCDS; CCDS58316.1; -. [Q96PC5-12]
DR CCDS; CCDS58317.1; -. [Q96PC5-13]
DR CCDS; CCDS86384.1; -. [Q96PC5-3]
DR CCDS; CCDS86385.1; -. [Q96PC5-10]
DR CCDS; CCDS86386.1; -. [Q96PC5-11]
DR CCDS; CCDS9672.1; -. [Q96PC5-2]
DR CCDS; CCDS9673.1; -. [Q96PC5-14]
DR CCDS; CCDS9674.1; -. [Q96PC5-7]
DR CCDS; CCDS9675.1; -. [Q96PC5-8]
DR CCDS; CCDS9676.1; -. [Q96PC5-9]
DR RefSeq; NP_001234917.1; NM_001247988.1. [Q96PC5-5]
DR RefSeq; NP_001234918.1; NM_001247989.1. [Q96PC5-12]
DR RefSeq; NP_001234919.1; NM_001247990.1. [Q96PC5-13]
DR RefSeq; NP_001316143.1; NM_001329214.1. [Q96PC5-3]
DR RefSeq; NP_005921.2; NM_005930.3. [Q96PC5-7]
DR RefSeq; NP_473365.3; NM_054024.3. [Q96PC5-2]
DR RefSeq; NP_976229.1; NM_203354.2. [Q96PC5-14]
DR RefSeq; NP_976231.1; NM_203356.2. [Q96PC5-9]
DR RefSeq; XP_006720211.1; XM_006720148.2.
DR RefSeq; XP_011535086.1; XM_011536784.2.
DR RefSeq; XP_011535087.1; XM_011536785.2. [Q96PC5-11]
DR RefSeq; XP_016876809.1; XM_017021320.1.
DR RefSeq; XP_016876814.1; XM_017021325.1.
DR AlphaFoldDB; Q96PC5; -.
DR SMR; Q96PC5; -.
DR BioGRID; 110409; 106.
DR BioGRID; 125559; 16.
DR IntAct; Q96PC5; 55.
DR MINT; Q96PC5; -.
DR STRING; 9606.ENSP00000452252; -.
DR TCDB; 9.B.113.1.4; the collagen secretory protein, mia3 (mia3) family.
DR GlyGen; Q96PC5; 3 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q96PC5; -.
DR PhosphoSitePlus; Q96PC5; -.
DR BioMuta; CTAGE5; -.
DR BioMuta; HGNC:18432; -.
DR DMDM; 308153584; -.
DR EPD; Q96PC5; -.
DR jPOST; Q96PC5; -.
DR MassIVE; Q96PC5; -.
DR MaxQB; Q96PC5; -.
DR PaxDb; Q96PC5; -.
DR PeptideAtlas; Q96PC5; -.
DR PRIDE; Q96PC5; -.
DR ProteomicsDB; 33711; -.
DR ProteomicsDB; 48581; -.
DR ProteomicsDB; 48582; -.
DR ProteomicsDB; 48583; -.
DR ProteomicsDB; 48584; -.
DR ProteomicsDB; 48585; -.
DR ProteomicsDB; 48586; -.
DR ProteomicsDB; 48587; -.
DR ProteomicsDB; 48588; -.
DR ProteomicsDB; 77665; -. [Q96PC5-2]
DR Antibodypedia; 79482; 343 antibodies from 27 providers.
DR DNASU; 4253; -.
DR Ensembl; ENST00000280082.4; ENSP00000280082.3; ENSG00000150527.18. [Q96PC5-2]
DR Ensembl; ENST00000280083.7; ENSP00000280083.3; ENSG00000150527.18. [Q96PC5-7]
DR Ensembl; ENST00000341502.9; ENSP00000339286.5; ENSG00000150527.18. [Q96PC5-10]
DR Ensembl; ENST00000341749.7; ENSP00000343897.3; ENSG00000150527.18. [Q96PC5-14]
DR Ensembl; ENST00000348007.7; ENSP00000343912.3; ENSG00000150527.18. [Q96PC5-8]
DR Ensembl; ENST00000396158.6; ENSP00000379462.2; ENSG00000150527.18. [Q96PC5-12]
DR Ensembl; ENST00000396165.8; ENSP00000379468.4; ENSG00000150527.18. [Q96PC5-9]
DR Ensembl; ENST00000553352.1; ENSP00000450449.1; ENSG00000150527.18. [Q96PC5-9]
DR Ensembl; ENST00000556148.5; ENSP00000452562.1; ENSG00000150527.18. [Q96PC5-13]
DR Ensembl; ENST00000557038.5; ENSP00000450869.1; ENSG00000150527.18. [Q96PC5-11]
DR Ensembl; ENST00000640607.2; ENSP00000491014.1; ENSG00000150527.18. [Q96PC5-3]
DR GeneID; 4253; -.
DR KEGG; hsa:4253; -.
DR MANE-Select; ENST00000640607.2; ENSP00000491014.1; NM_001329214.4; NP_001316143.1.
DR UCSC; uc001wux.4; human. [Q96PC5-3]
DR CTD; 4253; -.
DR DisGeNET; 4253; -.
DR GeneCards; MIA2; -.
DR HGNC; HGNC:18432; MIA2.
DR HPA; ENSG00000150527; Tissue enhanced (liver).
DR MIM; 602132; gene.
DR neXtProt; NX_Q96PC5; -.
DR OpenTargets; ENSG00000150527; -.
DR PharmGKB; PA134870998; -.
DR VEuPathDB; HostDB:ENSG00000150527; -.
DR eggNOG; ENOG502QUND; Eukaryota.
DR GeneTree; ENSGT00950000182767; -.
DR HOGENOM; CLU_028032_0_0_1; -.
DR InParanoid; Q96PC5; -.
DR OMA; GPDCLYL; -.
DR OrthoDB; 135910at2759; -.
DR TreeFam; TF332724; -.
DR TreeFam; TF333137; -.
DR PathwayCommons; Q96PC5; -.
DR Reactome; R-HSA-5694530; Cargo concentration in the ER.
DR SignaLink; Q96PC5; -.
DR BioGRID-ORCS; 4253; 34 hits in 1077 CRISPR screens.
DR ChiTaRS; MIA2; human.
DR GeneWiki; CTAGE5; -.
DR GeneWiki; MIA2; -.
DR GenomeRNAi; 4253; -.
DR Pharos; Q96PC5; Tbio.
DR PRO; PR:Q96PC5; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q96PC5; protein.
DR Bgee; ENSG00000150527; Expressed in right lobe of liver and 188 other tissues.
DR ExpressionAtlas; Q96PC5; baseline and differential.
DR Genevisible; Q96PC5; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IDA: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:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0038024; F:cargo receptor activity; IMP:UniProtKB.
DR GO; GO:0008047; F:enzyme activator activity; TAS:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:UniProtKB.
DR GO; GO:0042953; P:lipoprotein transport; IMP:UniProtKB.
DR GO; GO:0032527; P:protein exit from endoplasmic reticulum; IMP:UniProtKB.
DR GO; GO:0070973; P:protein localization to endoplasmic reticulum exit site; IMP:UniProtKB.
DR GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR GO; GO:0035459; P:vesicle cargo loading; IMP:UniProtKB.
DR CDD; cd11892; SH3_MIA2; 1.
DR InterPro; IPR035555; MIA2_SH3.
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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1412
FT /note="Melanoma inhibitory activity protein 2"
FT /id="PRO_0000019031"
FT TOPO_DOM 20..605
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT INTRAMEM 606..626
FT /evidence="ECO:0000255"
FT TOPO_DOM 627..646
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 647..667
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 668..1412
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 39..101
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 260..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..1258
FT /note="Mediates interaction with MIA3"
FT /evidence="ECO:0000269|PubMed:21525241"
FT REGION 1153..1304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1259..1412
FT /note="Proline-rich domain (PRD); mediates interaction with
FT the COPII coat subunits SEC23A and SEC23B"
FT /evidence="ECO:0000269|PubMed:21525241,
FT ECO:0000269|PubMed:27551091"
FT REGION 1316..1412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 725..850
FT /evidence="ECO:0000255"
FT COILED 948..1102
FT /evidence="ECO:0000255"
FT COMPBIAS 269..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..554
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1181..1195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1225..1245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1345..1359
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1365..1386
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 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..688
FT /note="Missing (in isoform 10 and isoform 12)"
FT /id="VSP_060003"
FT VAR_SEQ 1..637
FT /note="Missing (in isoform 4 and isoform 8)"
FT /id="VSP_060004"
FT VAR_SEQ 1..620
FT /note="Missing (in isoform 5 and isoform 13)"
FT /id="VSP_060005"
FT VAR_SEQ 1..608
FT /note="Missing (in isoform 6, isoform 7, isoform 9 and
FT isoform 11)"
FT /id="VSP_060006"
FT VAR_SEQ 609..628
FT /note="QIDVYDFMNSAFSPIVILTE -> MEEPGVTPQPYLGLLLEELR (in
FT isoform 6, isoform 7, isoform 9 and isoform 11)"
FT /id="VSP_060007"
FT VAR_SEQ 621..629
FT /note="SPIVILTER -> MELKSPEEE (in isoform 5 and isoform
FT 13)"
FT /id="VSP_060008"
FT VAR_SEQ 631..654
FT /note="VAALPEGMRPDSNLYGFPWELVIC -> SLPFKPFAIILPILLNIRVATKYV
FT (in isoform 2)"
FT /id="VSP_058472"
FT VAR_SEQ 655..1412
FT /note="Missing (in isoform 2)"
FT /id="VSP_058473"
FT VAR_SEQ 711..736
FT /note="Missing (in isoform 5)"
FT /id="VSP_060009"
FT VAR_SEQ 736
FT /note="E -> EVENQM (in isoform 11 and isoform 12)"
FT /id="VSP_060010"
FT VAR_SEQ 1123..1165
FT /note="Missing (in isoform 4 and isoform 7)"
FT /id="VSP_060011"
FT VAR_SEQ 1255..1325
FT /note="Missing (in isoform 5)"
FT /id="VSP_060012"
FT VAR_SEQ 1333..1355
FT /note="Missing (in isoform 5)"
FT /id="VSP_060013"
FT VAR_SEQ 1358..1379
FT /note="MRNVYPPRGFPPYLPPRPGFFP -> SARSPPGAGAPASGRGLGGPQK (in
FT isoform 9)"
FT /id="VSP_060014"
FT VAR_SEQ 1380..1412
FT /note="Missing (in isoform 9)"
FT /id="VSP_060015"
FT VARIANT 437
FT /note="D -> H (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036460"
FT VARIANT 813
FT /note="K -> N (in dbSNP:rs17855896)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_047891"
FT VARIANT 858
FT /note="K -> E (in dbSNP:rs10162564)"
FT /id="VAR_047892"
FT VARIANT 968
FT /note="E -> Q (in dbSNP:rs1950952)"
FT /evidence="ECO:0000269|PubMed:12839582,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:17974005,
FT ECO:0000269|PubMed:9356211"
FT /id="VAR_047893"
FT VARIANT 983
FT /note="N -> S (in dbSNP:rs17109109)"
FT /id="VAR_047894"
FT VARIANT 1307
FT /note="I -> V (in dbSNP:rs1140952)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9356211"
FT /id="VAR_047895"
FT VARIANT 1346
FT /note="G -> R (in dbSNP:rs1060878)"
FT /evidence="ECO:0000269|PubMed:12839582,
FT ECO:0000269|PubMed:17974005, ECO:0000269|PubMed:9356211"
FT /id="VAR_047896"
FT MUTAGEN 679
FT /note="Y->A: No effect on interaction with PERB."
FT /evidence="ECO:0000269|PubMed:27170179"
FT MUTAGEN 697
FT /note="K->A: Loss of interaction with PERB. Unable to
FT recruit PERB to the endoplasmic reticulum exit sites. Loss
FT of function in collagen VII transport. No effect on
FT interaction with MIA3."
FT /evidence="ECO:0000269|PubMed:27170179"
FT MUTAGEN 705
FT /note="S->A: Decreased interaction with PERB. No effect on
FT interaction with MIA3."
FT /evidence="ECO:0000269|PubMed:27170179"
FT MUTAGEN 720
FT /note="L->A: No effect on interaction with PERB."
FT /evidence="ECO:0000269|PubMed:27170179"
FT CONFLICT 83
FT /note="Missing (in Ref. 9; AAL26990)"
FT /evidence="ECO:0000305"
FT CONFLICT 698
FT /note="S -> N (in Ref. 5; CAE45997)"
FT /evidence="ECO:0000305"
FT CONFLICT 753
FT /note="I -> M (in Ref. 5; CAE45997)"
FT /evidence="ECO:0000305"
FT CONFLICT 803
FT /note="K -> Q (in Ref. 1; AAB86589/AAB86593)"
FT /evidence="ECO:0000305"
FT CONFLICT 806
FT /note="Q -> P (in Ref. 1; AAB86593)"
FT /evidence="ECO:0000305"
FT CONFLICT 1154
FT /note="R -> T (in Ref. 1; AAB86593)"
FT /evidence="ECO:0000305"
FT CONFLICT 1197
FT /note="P -> L (in Ref. 1; AAB86593)"
FT /evidence="ECO:0000305"
FT CONFLICT 1202
FT /note="S -> F (in Ref. 1; AAB86593)"
FT /evidence="ECO:0000305"
FT CONFLICT 1212
FT /note="R -> M (in Ref. 2; AAN77610)"
FT /evidence="ECO:0000305"
FT CONFLICT 1384
FT /note="S -> F (in Ref. 2; AAN77610)"
FT /evidence="ECO:0000305"
FT VARIANT Q96PC5-7:6
FT /note="V -> A (in dbSNP:rs7140561)"
FT /evidence="ECO:0000269|PubMed:9356211"
FT /id="VAR_082860"
FT VARIANT Q96PC5-8:6
FT /note="V -> A (in dbSNP:rs7140561)"
FT /evidence="ECO:0000269|PubMed:9356211"
FT /id="VAR_082861"
FT VARIANT Q96PC5-10:6
FT /note="V -> A (in dbSNP:rs7140561)"
FT /evidence="ECO:0000269|PubMed:12839582"
FT /id="VAR_082862"
FT VARIANT Q96PC5-12:6
FT /note="V -> A (in dbSNP:rs7140561)"
FT /evidence="ECO:0000305"
FT /id="VAR_082863"
FT VARIANT Q96PC5-12:11
FT /note="Y -> D (in dbSNP:rs17855895)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_082864"
SQ SEQUENCE 1412 AA; 159836 MW; E870056BF9D5A0B2 CRC64;
MAKFGVHRIL LLAISLTKCL ESTKLLADLK KCGDLECEAL INRVSAMRDY RGPDCRYLNF
TKGEEISVYV KLAGEREDLW AGSKGKEFGY FPRDAVQIEE VFISEEIQMS TKESDFLCLL
GVSYTFDNED SELNGDYGEN IYPYEEDKDE KSSIYESDFQ IEPGFYATYE STLFEDQVPA
LEAPEDIGST SESKDWEEVV VESMEQDRIP EVHVPPSSAV SGVKEWFGLG GEQAEEKAFE
SVIEPVQESS FRSRKIAVED ENDLEELNNG EPQTEHQQES ESEIDSVPKT QSELASESEH
IPKPQSTGWF GGGFTSYLGF GDEDTGLELI AEESNPPLQD FPNSISSDKE ATVPCTEILT
EKKDTITNDS LSLKPSWFDF GFAILGFAYA KEDKIMLDDR KNEEDGGADE HEHPLTSELD
PEKEQEIETI KIIETEDQID KKPVSEKTDE SDTIPYLKKF LYNFDNPWNF QNIPKETELP
FPKQILDQNN VIENEETGEF SIDNYPTDNT KVMIFKSSYS LSDMVSNIEL PTRIHEEVYF
EPSSSKDSDE NSKPSVDTEG PALVEIDRSV ENTLLNSQMV STDNSLSSQN YISQKEDASE
FQILKYLFQI DVYDFMNSAF SPIVILTERV VAALPEGMRP DSNLYGFPWE LVICAAVVGF
FAVLFFLWRS FRSVRSRLYV GREKKLALML SGLIEEKSKL LEKFSLVQKE YEGYEVESSL
KDASFEKEAT EAQSLEATCE KLNRSNSELE DEILCLEKEL KEEKSKHSEQ DELMADISKR
IQSLEDESKS LKSQVAEAKM TFKIFQMNEE RLKIAIKDAL NENSQLQESQ KQLLQEAEVW
KEQVSELNKQ KVTFEDSKVH AEQVLNDKES HIKTLTERLL KMKDWAAMLG EDITDDDNLE
LEMNSESENG AYLDNPPKGA LKKLIHAAKL NASLKTLEGE RNQIYIQLSE VDKTKEELTE
HIKNLQTEQA SLQSENTHFE NENQKLQQKL KVMTELYQEN EMKLHRKLTV EENYRLEKEE
KLSKVDEKIS HATEELETYR KRAKDLEEEL ERTIHSYQGQ IISHEKKAHD NWLAARNAER
NLNDLRKENA HNRQKLTETE LKFELLEKDP YALDVPNTAF GREHSPYGPS PLGWPSSETR
AFLSPPTLLE GPLRLSPLLP GGGGRGSRGP GNPLDHQITN ERGESSCDRL TDPHRAPSDT
GSLSPPWDQD RRMMFPPPGQ SYPDSALPPQ RQDRFCSNSG RLSGPAELRS FNMPSLDKMD
GSMPSEMESS RNDTKDDLGN LNVPDSSLPA ENEATGPGFV PPPLAPIRGP LFPVDARGPF
LRRGPPFPPP PPGAMFGASR DYFPPGDFPG PPPAPFAMRN VYPPRGFPPY LPPRPGFFPP
PPHSEGRSEF PSGLIPPSNE PATEHPEPQQ ET
