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 08-NOV-2023, entry version 165. 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 -!- 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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. 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; 108. DR BioGRID; 125559; 18. DR IntAct; Q96PC5; 57. DR STRING; 9606.ENSP00000452252; -. DR TCDB; 9.B.113.1.4; the collagen secretory protein, mia3 (mia3) family. DR GlyCosmos; Q96PC5; 3 sites, 1 glycan. DR GlyGen; Q96PC5; 4 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q96PC5; -. DR PhosphoSitePlus; Q96PC5; -. DR SwissPalm; 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; 9606-ENSP00000452252; -. DR PeptideAtlas; 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 Pumba; Q96PC5; -. DR Antibodypedia; 79482; 356 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 AGR; HGNC:18432; -. 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; TAHKAQY; -. DR OrthoDB; 5406966at2759; -. 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; 37 hits in 1155 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: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 Gene3D; 2.30.30.40; SH3 Domains; 1. DR InterPro; IPR035555; MIA2_SH3. 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..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 //