TGO1_HUMAN
ID TGO1_HUMAN Reviewed; 1907 AA.
AC Q5JRA6; A8K2S0; A8MT05; A8MT13; B7Z430; Q14083; Q3S4X3; Q5JRA5; Q5JRB0;
AC Q5JRB1; Q5JRB2; Q6UVY8; Q86Y60; Q8N8M5; Q92580;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Transport and Golgi organization protein 1 homolog {ECO:0000305};
DE Short=TANGO1 {ECO:0000303|PubMed:19269366};
DE AltName: Full=C219-reactive peptide {ECO:0000303|PubMed:7758977};
DE AltName: Full=D320 {ECO:0000303|PubMed:7758977};
DE AltName: Full=Melanoma inhibitory activity protein 3 {ECO:0000312|HGNC:HGNC:24008};
DE Flags: Precursor;
GN Name=MIA3 {ECO:0000312|HGNC:HGNC:24008};
GN Synonyms=KIAA0268 {ECO:0000312|EMBL:BAA13448.1},
GN TANGO {ECO:0000303|PubMed:15183315}; ORFNames=UNQ6077/PRO20088;
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 [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT GLU-482.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 419-1492 (ISOFORM 2).
RC TISSUE=Brain, 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-125, AND TISSUE SPECIFICITY.
RX PubMed=15183315; DOI=10.1016/j.modgep.2003.12.002;
RA Bosserhoff A.K., Moser M., Buettner R.;
RT "Characterization and expression pattern of the novel MIA homolog TANGO.";
RL Gene Expr. Patterns 4:473-479(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 715-1907 (ISOFORM 1), AND VARIANT
RP GLY-881.
RC TISSUE=Bone marrow;
RX PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. VI. The
RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of
RT cDNA clones from cell line KG-1 and brain.";
RL DNA Res. 3:321-329(1996).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1306-1441.
RC TISSUE=Leukemia;
RX PubMed=7758977; DOI=10.1016/0378-1119(94)00541-y;
RA Norris M.D., Gilbert J., Madafiglio J., Haber M.;
RT "Analysis of a novel cDNA encoding a C219-reactive peptide isolated from
RT methotrexate-selected multidrug-resistant human leukemic cells.";
RL Gene 156:313-314(1995).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1441-1907 (ISOFORM 1), AND
RP VARIANTS CYS-1659 AND GLU-1723.
RC TISSUE=Brain;
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 [8]
RP TISSUE SPECIFICITY.
RX PubMed=17044017; DOI=10.1002/ijc.22242;
RA Arndt S., Bosserhoff A.K.;
RT "TANGO is a tumor suppressor of malignant melanoma.";
RL Int. J. Cancer 119:2812-2820(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1906, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH COL7A1; SEC23A AND SEC24C,
RP TOPOLOGY, DOMAIN, AND REGION.
RX PubMed=19269366; DOI=10.1016/j.cell.2008.12.025;
RA Saito K., Chen M., Bard F., Chen S., Zhou H., Woodley D., Polischuk R.,
RA Schekman R., Malhotra V.;
RT "TANGO1 facilitates cargo loading at endoplasmic reticulum exit sites.";
RL Cell 136:891-902(2009).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-589.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP INTERACTION WITH MIA2, SUBCELLULAR LOCATION, 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1745, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1706, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727; SER-876; SER-1067;
RP SER-1706 AND SER-1906, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [19]
RP PHOSPHORYLATION AT SER-226; SER-229 AND SER-1906.
RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT "A single kinase generates the majority of the secreted phosphoproteome.";
RL Cell 161:1619-1632(2015).
RN [20]
RP FUNCTION, AND INTERACTION WITH APOB AND MIA2.
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 [21]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SEC16A AND SEC23A, AND
RP REGION SIR.
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 [22]
RP SUBCELLULAR LOCATION, AND INVOLVEMENT IN ODCD2.
RX PubMed=32101163; DOI=10.7554/elife.51319;
RA Lekszas C., Foresti O., Raote I., Liedtke D., Koenig E.M., Nanda I.,
RA Vona B., De Coster P., Cauwels R., Malhotra V., Haaf T.;
RT "Biallelic TANGO1 mutations cause a novel syndromal disease due to hampered
RT cellular collagen secretion.";
RL Elife 9:0-0(2020).
RN [23] {ECO:0007744|PDB:5KYN, ECO:0007744|PDB:5KYU, ECO:0007744|PDB:5KYW}
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 1796-1808 IN COMPLEX WITH SEC23A,
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).
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. This protein is required for collagen VII
CC (COL7A1) secretion by loading COL7A1 into transport carriers. It may
CC participate in cargo loading of COL7A1 at endoplasmic reticulum exit
CC sites by binding to COPII coat subunits Sec23/24 and guiding SH3-bound
CC COL7A1 into a growing carrier. Does not play a role in global protein
CC secretion and is apparently specific to COL7A1 cargo loading. However,
CC it may participate in secretion of other proteins in cells that do not
CC secrete COL7A1. It is also specifically required for the secretion of
CC lipoproteins by participating in their export from the endoplasmic
CC reticulum (PubMed:27138255, PubMed:19269366). Required for correct
CC assembly of COPII coat components at endoplasmic reticulum exit sites
CC (ERES) and for the localization of SEC16A and membrane-bound ER-
CC resident complexes consisting of MIA2 and PREB/SEC12 to ERES
CC (PubMed:28442536). {ECO:0000269|PubMed:19269366,
CC ECO:0000269|PubMed:27138255, ECO:0000269|PubMed:28442536}.
CC -!- SUBUNIT: Interacts with MIA2 (PubMed:21525241). Interacts (via SH3
CC domain) with COL7A1 (PubMed:19269366). Interacts with the COPII coat
CC subunits SEC23A, SEC23B and maybe SEC24C (PubMed:19269366,
CC PubMed:27551091, PubMed:28442536). May interact with APOB and MIA2
CC (PubMed:27138255). Isoform 1 and isoform 4 interact with SEC16A
CC (PubMed:28442536). {ECO:0000269|PubMed:19269366,
CC ECO:0000269|PubMed:21525241, ECO:0000269|PubMed:27138255,
CC ECO:0000269|PubMed:27551091, ECO:0000269|PubMed:28442536}.
CC -!- INTERACTION:
CC Q5JRA6; O95833: CLIC3; NbExp=3; IntAct=EBI-2291868, EBI-10192241;
CC Q5JRA6; Q02388: COL7A1; NbExp=2; IntAct=EBI-2291868, EBI-724237;
CC Q5JRA6; Q9NSC5: HOMER3; NbExp=3; IntAct=EBI-2291868, EBI-748420;
CC Q5JRA6; Q96PV6: LENG8; NbExp=3; IntAct=EBI-2291868, EBI-739546;
CC Q5JRA6; O43639: NCK2; NbExp=3; IntAct=EBI-2291868, EBI-713635;
CC Q5JRA6; Q15436: SEC23A; NbExp=3; IntAct=EBI-2291868, EBI-81088;
CC Q5JRA6-2; Q53EZ4: CEP55; NbExp=4; IntAct=EBI-10244342, EBI-747776;
CC Q5JRA6-2; P51116: FXR2; NbExp=3; IntAct=EBI-10244342, EBI-740459;
CC Q5JRA6-2; Q9GZV8: PRDM14; NbExp=3; IntAct=EBI-10244342, EBI-3957793;
CC Q5JRA6-2; P14373: TRIM27; NbExp=3; IntAct=EBI-10244342, EBI-719493;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:19269366, ECO:0000269|PubMed:21525241,
CC ECO:0000269|PubMed:32101163}; Single-pass membrane protein
CC {ECO:0000269|PubMed:19269366}. Note=Localizes at endoplasmic reticulum
CC exit sites (ERES), also known as transitional endoplasmic reticulum
CC (tER) (PubMed:32101163). SEC16A is required for its proper localization
CC to ERES. After loading of COL7A1 into transport carriers, it is not
CC incorporated into COPII carriers and remains in the endoplasmic
CC reticulum membrane. {ECO:0000269|PubMed:19269366,
CC ECO:0000269|PubMed:21525241, ECO:0000269|PubMed:28442536}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=TANGO1L {ECO:0000303|PubMed:28442536};
CC IsoId=Q5JRA6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5JRA6-2; Sequence=VSP_025864;
CC Name=3;
CC IsoId=Q5JRA6-3; Sequence=VSP_025861, VSP_025862;
CC Name=4; Synonyms=TANGO1S {ECO:0000303|PubMed:28442536};
CC IsoId=Q5JRA6-4; Sequence=VSP_025860, VSP_025863;
CC -!- TISSUE SPECIFICITY: Broadly expressed, except in bone marrow and
CC peripheral blood mononuclear cells. Down-regulated in melanoma tissue.
CC {ECO:0000269|PubMed:15183315, ECO:0000269|PubMed:17044017}.
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.
CC {ECO:0000269|PubMed:19269366, ECO:0000269|PubMed:27551091}.
CC -!- DOMAIN: Although 2 transmembrane domains are predicted, PubMed:19269366
CC showed that it only contains one transmembrane domain. The other
CC predicted transmembrane region is probably a hairpin-type region
CC embedded into the membrane, which does not cross the membrane. It is
CC unclear which of the 2 predicted transmembrane regions is the
CC transmembrane or the hairpin-type region.
CC {ECO:0000269|PubMed:19269366}.
CC -!- DISEASE: Odontochondrodysplasia 2 with hearing loss and diabetes
CC (ODCD2) [MIM:619269]: An autosomal recessive disorder characterized by
CC dentinogenesis imperfecta, delayed tooth eruption, growth retardation
CC with proportionate short stature, skeletal abnormalities, and
CC dysmorphic facies in association with insulin-dependent diabetes
CC mellitus, sensorineural hearing loss, and mild intellectual disability.
CC {ECO:0000269|PubMed:32101163}. Note=The disease may be caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the MIA/OTOR family. Tango1 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC04810.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAF83024.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY359091; AAQ89449.1; -; mRNA.
DR EMBL; AK096526; BAC04810.1; ALT_INIT; mRNA.
DR EMBL; AK290335; BAF83024.1; ALT_INIT; mRNA.
DR EMBL; AK296712; BAH12416.1; -; mRNA.
DR EMBL; AL592148; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; D87742; BAA13448.1; -; mRNA.
DR EMBL; L34688; AAB00324.1; -; mRNA.
DR EMBL; DQ166034; AAZ95512.1; -; mRNA.
DR EMBL; BC047116; AAH47116.2; -; mRNA.
DR CCDS; CCDS41470.1; -. [Q5JRA6-1]
DR CCDS; CCDS73035.1; -. [Q5JRA6-4]
DR RefSeq; NP_001287796.1; NM_001300867.1. [Q5JRA6-4]
DR RefSeq; NP_001310992.1; NM_001324063.1. [Q5JRA6-2]
DR RefSeq; NP_940953.2; NM_198551.3. [Q5JRA6-1]
DR PDB; 5KYN; X-ray; 2.55 A; C=1796-1803.
DR PDB; 5KYU; X-ray; 3.51 A; C=1796-1803.
DR PDB; 5KYW; X-ray; 3.20 A; C=1800-1808.
DR PDBsum; 5KYN; -.
DR PDBsum; 5KYU; -.
DR PDBsum; 5KYW; -.
DR AlphaFoldDB; Q5JRA6; -.
DR SMR; Q5JRA6; -.
DR BioGRID; 131952; 226.
DR CORUM; Q5JRA6; -.
DR IntAct; Q5JRA6; 50.
DR MINT; Q5JRA6; -.
DR STRING; 9606.ENSP00000340900; -.
DR TCDB; 9.B.113.1.2; the collagen secretory protein, mia3 (mia3) family.
DR GlyConnect; 1498; 8 N-Linked glycans (3 sites).
DR GlyGen; Q5JRA6; 11 sites, 7 N-linked glycans (3 sites), 2 O-linked glycans (7 sites).
DR iPTMnet; Q5JRA6; -.
DR MetOSite; Q5JRA6; -.
DR PhosphoSitePlus; Q5JRA6; -.
DR BioMuta; MIA3; -.
DR DMDM; 74741823; -.
DR EPD; Q5JRA6; -.
DR jPOST; Q5JRA6; -.
DR MassIVE; Q5JRA6; -.
DR MaxQB; Q5JRA6; -.
DR PaxDb; Q5JRA6; -.
DR PeptideAtlas; Q5JRA6; -.
DR PRIDE; Q5JRA6; -.
DR ProteomicsDB; 63078; -. [Q5JRA6-1]
DR ProteomicsDB; 63079; -. [Q5JRA6-2]
DR ProteomicsDB; 63080; -. [Q5JRA6-3]
DR ProteomicsDB; 63081; -. [Q5JRA6-4]
DR Antibodypedia; 53971; 103 antibodies from 28 providers.
DR DNASU; 375056; -.
DR Ensembl; ENST00000340535.11; ENSP00000345866.7; ENSG00000154305.18. [Q5JRA6-4]
DR Ensembl; ENST00000344922.10; ENSP00000340900.5; ENSG00000154305.18. [Q5JRA6-1]
DR GeneID; 375056; -.
DR KEGG; hsa:375056; -.
DR MANE-Select; ENST00000344922.10; ENSP00000340900.5; NM_198551.4; NP_940953.2.
DR UCSC; uc001hnl.4; human. [Q5JRA6-1]
DR CTD; 375056; -.
DR DisGeNET; 375056; -.
DR GeneCards; MIA3; -.
DR HGNC; HGNC:24008; MIA3.
DR HPA; ENSG00000154305; Low tissue specificity.
DR MIM; 613455; gene.
DR MIM; 619269; phenotype.
DR neXtProt; NX_Q5JRA6; -.
DR OpenTargets; ENSG00000154305; -.
DR PharmGKB; PA143485536; -.
DR VEuPathDB; HostDB:ENSG00000154305; -.
DR eggNOG; ENOG502QS87; Eukaryota.
DR GeneTree; ENSGT00950000182767; -.
DR HOGENOM; CLU_002106_1_0_1; -.
DR InParanoid; Q5JRA6; -.
DR OMA; APLMGDN; -.
DR OrthoDB; 208382at2759; -.
DR PhylomeDB; Q5JRA6; -.
DR TreeFam; TF333137; -.
DR PathwayCommons; Q5JRA6; -.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-HSA-5694530; Cargo concentration in the ER.
DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR SignaLink; Q5JRA6; -.
DR BioGRID-ORCS; 375056; 16 hits in 1070 CRISPR screens.
DR ChiTaRS; MIA3; human.
DR GenomeRNAi; 375056; -.
DR Pharos; Q5JRA6; Tbio.
DR PRO; PR:Q5JRA6; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5JRA6; protein.
DR Bgee; ENSG00000154305; Expressed in calcaneal tendon and 191 other tissues.
DR ExpressionAtlas; Q5JRA6; baseline and differential.
DR Genevisible; Q5JRA6; HS.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IDA:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0038024; F:cargo receptor activity; IMP:UniProtKB.
DR GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; IMP:BHF-UCL.
DR GO; GO:0140052; P:cellular response to oxidised low-density lipoprotein particle stimulus; IMP:BHF-UCL.
DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; IMP:UniProtKB.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IMP:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:UniProtKB.
DR GO; GO:0006887; P:exocytosis; IMP:UniProtKB.
DR GO; GO:0042953; P:lipoprotein transport; IMP:UniProtKB.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IDA:BHF-UCL.
DR GO; GO:0030336; P:negative regulation of cell migration; IDA:BHF-UCL.
DR GO; GO:1903038; P:negative regulation of leukocyte cell-cell adhesion; IMP:BHF-UCL.
DR GO; GO:2000402; P:negative regulation of lymphocyte migration; IMP:BHF-UCL.
DR GO; GO:0002687; P:positive regulation of leukocyte migration; IDA:BHF-UCL.
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:0015031; P:protein transport; IMP:UniProtKB.
DR GO; GO:0035459; P:vesicle cargo loading; IBA:GO_Central.
DR GO; GO:0042060; P:wound healing; IDA:BHF-UCL.
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 3D-structure; Alternative splicing; Coiled coil; Deafness;
KW Diabetes mellitus; Dwarfism; Endoplasmic reticulum; ER-Golgi transport;
KW Exocytosis; Glycoprotein; Intellectual disability; Membrane; Methylation;
KW Phosphoprotein; Protein transport; Reference proteome; SH3 domain; Signal;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1907
FT /note="Transport and Golgi organization protein 1 homolog"
FT /id="PRO_0000288998"
FT TOPO_DOM 23..1144
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT INTRAMEM 1145..1165
FT /evidence="ECO:0000255"
FT TOPO_DOM 1166..1176
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1177..1197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1198..1907
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 45..107
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 155..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1093..1121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1211..1650
FT /note="Mediates interaction with MIA2"
FT /evidence="ECO:0000269|PubMed:21525241"
FT REGION 1420..1443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1642..1907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1751..1907
FT /note="Proline-rich domain (PRD); mediates interaction with
FT the COPII coat subunits SEC23A and SEC23B"
FT /evidence="ECO:0000269|PubMed:19269366,
FT ECO:0000269|PubMed:27551091, ECO:0000269|PubMed:28442536"
FT REGION 1788..1847
FT /note="SEC16A-interacting region (SIR); required for its
FT localization to endoplasmic reticulum exit sites and for
FT its interaction with SEC16A"
FT /evidence="ECO:0000269|PubMed:28442536"
FT COILED 471..531
FT /evidence="ECO:0000255"
FT COILED 1214..1396
FT /evidence="ECO:0000255"
FT COILED 1487..1639
FT /evidence="ECO:0000255"
FT COMPBIAS 157..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..550
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..696
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..748
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..786
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..830
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..886
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..918
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1655..1671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1724..1747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1759..1809
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1856..1878
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1887..1907
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 226
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT MOD_RES 229
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT MOD_RES 727
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 876
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1067
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1431
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BI84"
FT MOD_RES 1666
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BI84"
FT MOD_RES 1678
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BI84"
FT MOD_RES 1706
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1727
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BI84"
FT MOD_RES 1741
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BI84"
FT MOD_RES 1745
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1784
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8BI84"
FT MOD_RES 1892
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BI84"
FT MOD_RES 1906
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:24275569"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 589
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT VAR_SEQ 1..1122
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_025860"
FT VAR_SEQ 493..500
FT /note="MTVHSSVH -> FKTEPIKL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_025861"
FT VAR_SEQ 501..1907
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_025862"
FT VAR_SEQ 1123..1159
FT /note="IDANKQPETAAEEPASVTPLENAILLIYSFMFYLTKS -> MDSVPATVPSI
FT AATPGDPELVGPLSVLYAAFIAKLLE (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_025863"
FT VAR_SEQ 1304..1362
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_025864"
FT VARIANT 482
FT /note="K -> E (in dbSNP:rs2936053)"
FT /evidence="ECO:0000269|PubMed:12975309"
FT /id="VAR_032546"
FT VARIANT 605
FT /note="K -> R (in dbSNP:rs2936052)"
FT /id="VAR_032547"
FT VARIANT 881
FT /note="E -> G (in dbSNP:rs2936051)"
FT /evidence="ECO:0000269|PubMed:9039502"
FT /id="VAR_032548"
FT VARIANT 1659
FT /note="G -> C (in dbSNP:rs17857325)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_032549"
FT VARIANT 1723
FT /note="K -> E (in dbSNP:rs17854428)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_032550"
FT CONFLICT 46
FT /note="Missing (in Ref. 1; AAQ89449)"
FT /evidence="ECO:0000305"
FT CONFLICT 1032
FT /note="H -> R (in Ref. 2; BAC04810)"
FT /evidence="ECO:0000305"
FT CONFLICT 1443
FT /note="R -> Q (in Ref. 7; AAH47116)"
FT /evidence="ECO:0000305"
FT CONFLICT 1754
FT /note="K -> R (in Ref. 2; BAH12416)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1907 AA; 213702 MW; D19C9AF1656F4B1C CRC64;
MAAAPGLLVW LLVLRLPWRV PGQLDPSTGR RFSEHKLCAD DECSMLMYRG EALEDFTGPD
CRFVNFKKGD PVYVYYKLAR GWPEVWAGSV GRTFGYFPKD LIQVVHEYTK EELQVPTDET
DFVCFDGGRD DFHNYNVEEL LGFLELYNSA ATDSEKAVEK TLQDMEKNPE LSKEREPEPE
PVEANSEESD SVFSENTEDL QEQFTTQKHH SHANSQANHA QGEQASFESF EEMLQDKLKV
PESENNKTSN SSQVSNEQDK IDAYKLLKKE MTLDLKTKFG STADALVSDD ETTRLVTSLE
DDFDEELDTE YYAVGKEDEE NQEDFDELPL LTFTDGEDMK TPAKSGVEKY PTDKEQNSNE
EDKVQLTVPP GIKNDDKNIL TTWGDTIFSI VTGGEETRDT MDLESSSSEE EKEDDDDALV
PDSKQGKPQS ATDYSDPDNV DDGLFIVDIP KTNNDKEVNA EHHIKGKGRG VQESKRGLVQ
DKTELEDENQ EGMTVHSSVH SNNLNSMPAA EKGKDTLKSA YDDTENDLKG AAIHISKGML
HEEKPGEQIL EGGSESESAQ KAAGNQMNDR KIQQESLGSA PLMGDDHPNA SRDSVEGDAL
VNGAKLHTLS VEHQREELKE ELVLKTQNQP RFSSPDEIDL PRELEDEVPI LGRNLPWQQE
RDVAATASKQ MSEKIRLSEG EAKEDSLDEE FFHHKAMQGT EVGQTDQTDS TGGPAFLSKV
EEDDYPSEEL LEDENAINAK RSKEKNPGNQ GRQFDVNLQV PDRAVLGTIH PDPEIEESKQ
ETSMILDSEK TSETAAKGVN TGGREPNTMV EKERPLADKK AQRPFERSDF SDSIKIQTPE
LGEVFQNKDS DYLKNDNPEE HLKTSGLAGE PEGELSKEDH ENTEKYMGTE SQGSAAAEPE
DDSFHWTPHT SVEPGHSDKR EDLLIISSFF KEQQSLQRFQ KYFNVHELEA LLQEMSSKLK
SAQQESLPYN MEKVLDKVFR ASESQILSIA EKMLDTRVAE NRDLGMNENN IFEEAAVLDD
IQDLIYFVRY KHSTAEETAT LVMAPPLEEG LGGAMEEMQP LHEDNFSREK TAELNVQVPE
EPTHLDQRVI GDTHASEVSQ KPNTEKDLDP GPVTTEDTPM DAIDANKQPE TAAEEPASVT
PLENAILLIY SFMFYLTKSL VATLPDDVQP GPDFYGLPWK PVFITAFLGI ASFAIFLWRT
VLVVKDRVYQ VTEQQISEKL KTIMKENTEL VQKLSNYEQK IKESKKHVQE TRKQNMILSD
EAIKYKDKIK TLEKNQEILD DTAKNLRVML ESEREQNVKN QDLISENKKS IEKLKDVISM
NASEFSEVQI ALNEAKLSEE KVKSECHRVQ EENARLKKKK EQLQQEIEDW SKLHAELSEQ
IKSFEKSQKD LEVALTHKDD NINALTNCIT QLNLLECESE SEGQNKGGND SDELANGEVG
GDRNEKMKNQ IKQMMDVSRT QTAISVVEED LKLLQLKLRA SVSTKCNLED QVKKLEDDRN
SLQAAKAGLE DECKTLRQKV EILNELYQQK EMALQKKLSQ EEYERQEREH RLSAADEKAV
SAAEEVKTYK RRIEEMEDEL QKTERSFKNQ IATHEKKAHE NWLKARAAER AIAEEKREAA
NLRHKLLELT QKMAMLQEEP VIVKPMPGKP NTQNPPRRGP LSQNGSFGPS PVSGGECSPP
LTVEPPVRPL SATLNRRDMP RSEFGSVDGP LPHPRWSAEA SGKPSPSDPG SGTATMMNSS
SRGSSPTRVL DEGKVNMAPK GPPPFPGVPL MSTPMGGPVP PPIRYGPPPQ LCGPFGPRPL
PPPFGPGMRP PLGLREFAPG VPPGRRDLPL HPRGFLPGHA PFRPLGSLGP REYFIPGTRL
PPPTHGPQEY PPPPAVRDLL PSGSRDEPPP ASQSTSQDCS QALKQSP
