SC16A_HUMAN
ID SC16A_HUMAN Reviewed; 2357 AA.
AC O15027; A1YCA4; J3KNL6; Q4G0D7; Q5SXP0; Q5SXP1; Q8N347; Q96HP1;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2018, sequence version 4.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Protein transport protein Sec16A;
DE AltName: Full=SEC16 homolog A;
DE Short=p250 {ECO:0000303|PubMed:17428803};
GN Name=SEC16A; Synonyms=KIAA0310, SEC16, SEC16L;
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 1).
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [3]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R., Nomura N.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 179-2357 (ISOFORM 4), FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH SEC23A.
RC TISSUE=Liver;
RX PubMed=17192411; DOI=10.1091/mbc.e06-08-0707;
RA Bhattacharyya D., Glick B.S.;
RT "Two mammalian Sec16 homologues have nonredundant functions in endoplasmic
RT reticulum (ER) export and transitional ER organization.";
RL Mol. Biol. Cell 18:839-849(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1607-2357 (ISOFORM 1), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1276-2357 (ISOFORM 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1844-2357 (ISOFORM 5).
RC TISSUE=Lung, Placenta, and Testis;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314 AND SER-1964, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1964; SER-2022 AND SER-2083,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17005010; DOI=10.1111/j.1600-0854.2006.00493.x;
RA Watson P., Townley A.K., Koka P., Palmer K.J., Stephens D.J.;
RT "Sec16 defines endoplasmic reticulum exit sites and is required for
RT secretory cargo export in mammalian cells.";
RL Traffic 7:1678-1687(2006).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SEC23A AND SEC13.
RX PubMed=17428803; DOI=10.1074/jbc.m611237200;
RA Iinuma T., Shiga A., Nakamoto K., O'Brien M.B., Aridor M., Arimitsu N.,
RA Tagaya M., Tani K.;
RT "Mammalian Sec16/p250 plays a role in membrane traffic from the endoplasmic
RT reticulum.";
RL J. Biol. Chem. 282:17632-17639(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314 AND SER-1964, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1964 AND SER-2022, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569; SER-589; SER-592;
RP THR-593; SER-595; SER-1327; SER-1964; SER-2022; THR-2054 AND SER-2083, AND
RP IDENTIFICATION BY 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 [14]
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 [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SEC13.
RX PubMed=19638414; DOI=10.1242/jcs.044032;
RA Hughes H., Budnik A., Schmidt K., Palmer K.J., Mantell J., Noakes C.,
RA Johnson A., Carter D.A., Verkade P., Watson P., Stephens D.J.;
RT "Organisation of human ER-exit sites: requirements for the localisation of
RT Sec16 to transitional ER.";
RL J. Cell Sci. 122:2924-2934(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1964, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1964; SER-2022; SER-2042 AND
RP SER-2083, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314; SER-1069; SER-1356;
RP SER-1964; SER-2022; THR-2054; SER-2073 AND SER-2083, AND IDENTIFICATION BY
RP 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 [20]
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 [21]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21768384; DOI=10.1073/pnas.1103283108;
RA Yonekawa S., Furuno A., Baba T., Fujiki Y., Ogasawara Y., Yamamoto A.,
RA Tagaya M., Tani K.;
RT "Sec16B is involved in the endoplasmic reticulum export of the peroxisomal
RT membrane biogenesis factor peroxin 16 (Pex16) in mammalian cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12746-12751(2011).
RN [22]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SEC16B.
RX PubMed=22355596; DOI=10.1038/srep00077;
RA Budnik A., Heesom K.J., Stephens D.J.;
RT "Characterization of human Sec16B: indications of specialized, non-
RT redundant functions.";
RL Sci. Rep. 1:77-77(2011).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1356; SER-1359 AND SER-1362,
RP AND IDENTIFICATION BY 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 [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314; SER-331; SER-587;
RP SER-595; SER-1069; SER-1207; SER-1229; SER-1305; SER-1327; SER-1356;
RP SER-1369; SER-1964; THR-2054; SER-2056; SER-2073; SER-2083; SER-2271 AND
RP SER-2291, AND IDENTIFICATION BY 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 [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-559; SER-595;
RP SER-1069; THR-1325; SER-1347; SER-1350; SER-1356; SER-1359; SER-1573;
RP SER-1601; THR-1907; SER-1939; SER-1964; THR-2054; SER-2083 AND SER-2271,
RP AND 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 [26]
RP INTERACTION WITH LRRK2 AND SEC13, DOMAIN CCD, AND SUBCELLULAR LOCATION.
RX PubMed=25201882; DOI=10.15252/embj.201487807;
RA Cho H.J., Yu J., Xie C., Rudrabhatla P., Chen X., Wu J., Parisiadou L.,
RA Liu G., Sun L., Ma B., Ding J., Liu Z., Cai H.;
RT "Leucine-rich repeat kinase 2 regulates Sec16A at ER exit sites to allow
RT ER-Golgi export.";
RL EMBO J. 33:2314-2331(2014).
RN [27]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MIA3.
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 [28]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH GORASP2.
RX PubMed=28067262; DOI=10.1038/srep39887;
RA Piao H., Kim J., Noh S.H., Kweon H.S., Kim J.Y., Lee M.G.;
RT "Sec16A is critical for both conventional and unconventional secretion of
RT CFTR.";
RL Sci. Rep. 7:39887-39887(2017).
RN [29]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN CCD, AND INTERACTION WITH RNF183 AND
RP RNF152.
RX PubMed=29300766; DOI=10.1371/journal.pone.0190407;
RA Wu Y., Guo X.P., Kanemoto S., Maeoka Y., Saito A., Asada R., Matsuhisa K.,
RA Ohtake Y., Imaizumi K., Kaneko M.;
RT "Sec16A, a key protein in COPII vesicle formation, regulates the stability
RT and localization of the novel ubiquitin ligase RNF183.";
RL PLoS ONE 13:E0190407-E0190407(2018).
CC -!- FUNCTION: Acts as a molecular scaffold that plays a key role in the
CC organization of the endoplasmic reticulum exit sites (ERES), also known
CC as transitional endoplasmic reticulum (tER). SAR1A-GTP-dependent
CC assembly of SEC16A on the ER membrane forms an organized scaffold
CC defining an ERES. Required for secretory cargo traffic from the
CC endoplasmic reticulum to the Golgi apparatus (PubMed:17192411,
CC PubMed:17005010, PubMed:17428803, PubMed:21768384, PubMed:22355596).
CC Mediates the recruitment of MIA3/TANGO to ERES (PubMed:28442536).
CC Regulates both conventional (ER/Golgi-dependent) and GORASP2-mediated
CC unconventional (ER/Golgi-independent) trafficking of CFTR to cell
CC membrane (PubMed:28067262). Positively regulates the protein stability
CC of E3 ubiquitin-protein ligases RNF152 and RNF183 and the ER
CC localization of RNF183 (PubMed:29300766). Acts as a RAB10 effector in
CC the regulation of insulin-induced SLC2A4/GLUT4 glucose transporter-
CC enriched vesicles delivery to the cell membrane in adipocytes (By
CC similarity). {ECO:0000250|UniProtKB:E9QAT4,
CC ECO:0000269|PubMed:17005010, ECO:0000269|PubMed:17192411,
CC ECO:0000269|PubMed:17428803, ECO:0000269|PubMed:21768384,
CC ECO:0000269|PubMed:22355596, ECO:0000269|PubMed:28067262,
CC ECO:0000269|PubMed:28442536, ECO:0000269|PubMed:29300766}.
CC -!- SUBUNIT: SEC16A and SEC16B are each present in multiple copies in a
CC heteromeric complex (PubMed:17192411, PubMed:22355596). Interacts with
CC SEC23A (PubMed:17192411, PubMed:17428803). Interacts with RNF183 and
CC RNF152 (PubMed:29300766). Interacts with LRRK2 (via ROC domain)
CC (PubMed:25201882). Interacts with SEC13 (PubMed:25201882,
CC PubMed:19638414, PubMed:17428803). Interacts with RAB10 (By
CC similarity). Interacts with MIA3 (PubMed:28442536). Interacts with
CC GORASP2 in response to ER stress (PubMed:28067262).
CC {ECO:0000250|UniProtKB:E9QAT4, ECO:0000269|PubMed:17192411,
CC ECO:0000269|PubMed:17428803, ECO:0000269|PubMed:19638414,
CC ECO:0000269|PubMed:22355596, ECO:0000269|PubMed:25201882,
CC ECO:0000269|PubMed:28067262, ECO:0000269|PubMed:28442536,
CC ECO:0000269|PubMed:29300766}.
CC -!- INTERACTION:
CC O15027; Q96N67: DOCK7; NbExp=3; IntAct=EBI-357515, EBI-2433703;
CC O15027; Q5S007: LRRK2; NbExp=8; IntAct=EBI-357515, EBI-5323863;
CC O15027; Q6ZNJ1: NBEAL2; NbExp=6; IntAct=EBI-357515, EBI-2862306;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:17005010, ECO:0000269|PubMed:29300766}; Peripheral
CC membrane protein {ECO:0000269|PubMed:17005010}. Golgi apparatus
CC membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:E9QAT4}.
CC Cytoplasm, cytosol {ECO:0000269|PubMed:17428803,
CC ECO:0000269|PubMed:21768384}. Microsome membrane
CC {ECO:0000269|PubMed:17428803}. Note=SAR1A activity is required to
CC maintain SEC16A localization at discrete locations on the ER membrane
CC perhaps by preventing its dissociation (PubMed:17192411). Localizes to
CC endoplasmic reticulum exit sites (ERES), also known as transitional
CC endoplasmic reticulum (tER). MIA3 and LRRK2 are required for its proper
CC localization to ERES (PubMed:25201882, PubMed:28442536,
CC PubMed:19638414, PubMed:17428803, PubMed:22355596). Recruited to
CC microsomal membrane in SAR1-dependent manner (PubMed:17428803).
CC {ECO:0000269|PubMed:17192411, ECO:0000269|PubMed:17428803,
CC ECO:0000269|PubMed:19638414, ECO:0000269|PubMed:22355596,
CC ECO:0000269|PubMed:25201882, ECO:0000269|PubMed:28442536}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=O15027-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15027-2; Sequence=VSP_015252;
CC Name=3;
CC IsoId=O15027-3; Sequence=VSP_015253;
CC Name=4;
CC IsoId=O15027-4; Sequence=VSP_034370;
CC Name=5;
CC IsoId=O15027-5; Sequence=VSP_036029;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed at higher levels in the
CC pancreas. {ECO:0000269|PubMed:17192411}.
CC -!- SIMILARITY: Belongs to the SEC16 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA20769.4; Type=Erroneous initiation; Note=Extended 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; AB002308; BAA20769.4; ALT_INIT; mRNA.
DR EMBL; AL592301; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DQ903855; ABI78944.1; -; mRNA.
DR EMBL; BC008332; AAH08332.1; -; mRNA.
DR EMBL; BC028183; AAH28183.1; -; mRNA.
DR EMBL; BC098454; AAH98454.1; -; mRNA.
DR CCDS; CCDS55351.1; -. [O15027-1]
DR RefSeq; NP_001263347.1; NM_001276418.1.
DR RefSeq; NP_055681.1; NM_014866.1. [O15027-1]
DR RefSeq; XP_005266191.1; XM_005266134.2. [O15027-5]
DR RefSeq; XP_011517548.1; XM_011519246.2. [O15027-5]
DR RefSeq; XP_011517549.1; XM_011519247.1. [O15027-5]
DR RefSeq; XP_011517550.1; XM_011519248.2. [O15027-5]
DR RefSeq; XP_011517554.1; XM_011519252.2. [O15027-1]
DR RefSeq; XP_011517557.1; XM_011519255.2. [O15027-3]
DR RefSeq; XP_011517559.1; XM_011519257.1. [O15027-4]
DR RefSeq; XP_011517561.1; XM_011519259.1. [O15027-2]
DR RefSeq; XP_011517562.1; XM_011519260.2. [O15027-5]
DR AlphaFoldDB; O15027; -.
DR BioGRID; 115247; 356.
DR CORUM; O15027; -.
DR DIP; DIP-27588N; -.
DR IntAct; O15027; 239.
DR MINT; O15027; -.
DR STRING; 9606.ENSP00000325827; -.
DR ChEMBL; CHEMBL4295654; -.
DR GlyGen; O15027; 5 sites, 1 O-linked glycan (5 sites).
DR iPTMnet; O15027; -.
DR PhosphoSitePlus; O15027; -.
DR BioMuta; SEC16A; -.
DR EPD; O15027; -.
DR jPOST; O15027; -.
DR MassIVE; O15027; -.
DR MaxQB; O15027; -.
DR PaxDb; O15027; -.
DR PeptideAtlas; O15027; -.
DR PRIDE; O15027; -.
DR ProteomicsDB; 48383; -. [O15027-1]
DR ProteomicsDB; 48384; -. [O15027-2]
DR ProteomicsDB; 48385; -. [O15027-3]
DR ProteomicsDB; 48386; -. [O15027-4]
DR ProteomicsDB; 48387; -. [O15027-5]
DR Antibodypedia; 1693; 54 antibodies from 19 providers.
DR DNASU; 9919; -.
DR Ensembl; ENST00000313050.11; ENSP00000325827.7; ENSG00000148396.19. [O15027-1]
DR Ensembl; ENST00000684901.1; ENSP00000508822.1; ENSG00000148396.19. [O15027-1]
DR GeneID; 9919; -.
DR KEGG; hsa:9919; -.
DR MANE-Select; ENST00000684901.1; ENSP00000508822.1; NM_014866.2; NP_055681.1.
DR UCSC; uc064xch.1; human. [O15027-1]
DR CTD; 9919; -.
DR DisGeNET; 9919; -.
DR GeneCards; SEC16A; -.
DR HGNC; HGNC:29006; SEC16A.
DR HPA; ENSG00000148396; Low tissue specificity.
DR MIM; 612854; gene.
DR neXtProt; NX_O15027; -.
DR OpenTargets; ENSG00000148396; -.
DR PharmGKB; PA162402611; -.
DR VEuPathDB; HostDB:ENSG00000148396; -.
DR eggNOG; KOG1913; Eukaryota.
DR GeneTree; ENSGT00940000159324; -.
DR HOGENOM; CLU_001465_0_0_1; -.
DR InParanoid; O15027; -.
DR OMA; LERWKGA; -.
DR OrthoDB; 235062at2759; -.
DR PhylomeDB; O15027; -.
DR TreeFam; TF316276; -.
DR PathwayCommons; O15027; -.
DR Reactome; R-HSA-204005; COPII-mediated vesicle transport.
DR SignaLink; O15027; -.
DR SIGNOR; O15027; -.
DR BioGRID-ORCS; 9919; 412 hits in 1045 CRISPR screens.
DR ChiTaRS; SEC16A; human.
DR GeneWiki; SEC16A; -.
DR GenomeRNAi; 9919; -.
DR Pharos; O15027; Tbio.
DR PRO; PR:O15027; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; O15027; protein.
DR Bgee; ENSG00000148396; Expressed in endometrium epithelium and 203 other tissues.
DR ExpressionAtlas; O15027; baseline and differential.
DR Genevisible; O15027; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031090; C:organelle membrane; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0006914; P:autophagy; IEA:InterPro.
DR GO; GO:0048208; P:COPII vesicle coating; IEA:InterPro.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IDA:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0043000; P:Golgi to plasma membrane CFTR protein transport; IMP:UniProtKB.
DR GO; GO:0032527; P:protein exit from endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0070973; P:protein localization to endoplasmic reticulum exit site; IMP:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:UniProtKB.
DR GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB.
DR InterPro; IPR024298; ACE1_Sec16_Sec31.
DR InterPro; IPR024880; Sec16.
DR InterPro; IPR024340; Sec16_CCD.
DR PANTHER; PTHR13402; PTHR13402; 1.
DR Pfam; PF12932; Sec16; 1.
DR Pfam; PF12931; Sec16_C; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Endoplasmic reticulum; ER-Golgi transport;
KW Golgi apparatus; Membrane; Microsome; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..2357
FT /note="Protein transport protein Sec16A"
FT /id="PRO_0000050746"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 924..987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1006..1038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1019..1890
FT /note="Required for localization to endoplasmic reticulum
FT exit sites"
FT /evidence="ECO:0000269|PubMed:19638414"
FT REGION 1059..1151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1101..1400
FT /note="Interaction with MIA3"
FT /evidence="ECO:0000269|PubMed:28442536"
FT REGION 1102..1405
FT /note="Required for endoplasmic reticulum localization"
FT /evidence="ECO:0000269|PubMed:17192411"
FT REGION 1215..1248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1307..1378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1434..1890
FT /note="Central conserved domain (CCD); mediates interaction
FT with RNF183, LRRK2 and SEC13"
FT /evidence="ECO:0000269|PubMed:19638414,
FT ECO:0000269|PubMed:25201882, ECO:0000269|PubMed:29300766"
FT REGION 2049..2110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2106..2357
FT /note="Required for interaction with SEC23A"
FT /evidence="ECO:0000269|PubMed:17192411"
FT REGION 2141..2181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2226..2328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..781
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..828
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1006..1029
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1083..1105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1113..1136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1307..1356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1357..1378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2091..2110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2153..2176
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2272..2307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 559
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 569
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 587
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 589
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 592
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 593
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 595
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1069
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1305
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1325
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1327
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1347
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1350
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1356
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1359
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1369
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1573
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1601
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1907
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1939
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1964
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 2022
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES 2042
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 2054
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 2056
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2073
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2083
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 2271
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 2291
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 2231
FT /note="T -> TPVSSVRPQGRSGRNDGLLALSS (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036029"
FT VAR_SEQ 2265..2309
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_015252"
FT VAR_SEQ 2265..2289
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17192411"
FT /id="VSP_034370"
FT VAR_SEQ 2290..2309
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015253"
FT VARIANT 1039
FT /note="R -> C (in dbSNP:rs3812594)"
FT /id="VAR_023332"
FT CONFLICT 1277
FT /note="Y -> A (in Ref. 6; AAH28183)"
FT /evidence="ECO:0000305"
FT CONFLICT 2279
FT /note="S -> P (in Ref. 6; AAH28183)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2357 AA; 251894 MW; EAE9570BD5CD434B CRC64;
MQPPPQTVPS GMAGPPPAGN PRSVFWASSP YRRRANNNAA VAPTTCPLQP VTDPFAFSRQ
ALQSTPLGSS SKSSPPVLQG PAPAGFSQHP GLLVPHTHAR DSSQGPCEPL PGPLTQPRAH
ASPFSGALTP SAPPGPEMNR SAEVGPSSEP EVQTLPYLPH YIPGVDPETS HGGHPHGNMP
GLDRPLSRQN PHDGVVTPAA SPSLPQPGLQ MPGQWGPVQG GPQPSGQHRS PCPEGPVPSG
VPCATSVPHF PTPSILHQGP GHEQHSPLVA PPAALPSDGR DEVSHLQSGS HLANNSDPES
TFRQNPRIVN HWASPELRQN PGVKNEHRPA SALVNPLARG DSPENRTHHP LGAGAGSGCA
PLEADSGASG ALAMFFQGGE TENEENLSSE KAGLSGQADF DDFCSSPGLG RPPAPTHVGA
GSLCQALLPG PSNEAAGDVW GDTASTGVPD ASGSQYENVE NLEFVQNQEV LPSEPLNLDP
SSPSDQFRYG PLPGPAVPRH GAVCHTGAPD ATLHTVHPDS VSSSYSSRSH GRLSGSARPQ
ELVGTFIQQE VGKPEDEASG SFFKQIDSSP VGGETDETTV SQNYRGSVSQ PSTPSPPKPT
GIFQTSANSS FEPVKSHLVG VKPFEADRAN VVGEVRETCV RQKQCRPAAA LPDASPGNLE
QPPDNMETLC APQVCPLPLN STTEAVHMLP HAGAPPLDTV YPAPEKRPSA RTQGPVKCES
PATTLWAQSE LPDFGGNVLL APAAPALYVC AKPQPPVVQP PEEAMSGQQS RNPSSAAPVQ
SRGGIGASEN LENPPKMGEE EALQSQASSG YASLLSSPPT ESLQNPPVLI AQPDHSYNLA
QPINFSVSLS NSHEKNQSWR EALVGDRPAV SSWALGGDSG ENTSLSGIPT SSVLSLSLPS
SVAQSNFPQG SGASEMVSNQ PANLLVQPPS QPVPENLVPE SQKDRKAGSA LPGFANSPAG
STSVVLVPPA HGTLVPDGNK ANHSSHQEDT YGALDFTLSR TLENPVNVYN PSHSDSLASQ
QSVASHPRQS GPGAPNLDRF YQQVTKDAQG QPGLERAQQE LVPPQQQASP PQLPKAMFSE
LSNPESLPAQ GQAQNSAQSP ASLVLVDAGQ QLPPRPPQSS SVSLVSSGSG QAAVPSEQPW
PQPVPALAPG PPPQDLAAYY YYRPLYDAYQ PQYSLPYPPE PGAASLYYQD VYSLYEPRYR
PYDGAASAYA QNYRYPEPER PSSRASHSSE RPPPRQGYPE GYYSSKSGWS SQSDYYASYY
SSQYDYGDPG HWDRYHYSAR VRDPRTYDRR YWCDAEYDAY RREHSAFGDR PEKRDNNWRY
DPRFTGSFDD DPDPHRDPYG EEVDRRSVHS EHSARSLHSA HSLASRRSSL SSHSHQSQIY
RSHNVAAGSY EAPLPPGSFH GDFAYGTYRS NFSSGPGFPE YGYPADTVWP AMEQVSSRPT
SPEKFSVPHV CARFGPGGQL IKVIPNLPSE GQPALVEVHS MEALLQHTSE QEEMRAFPGP
LAKDDTHKVD VINFAQNKAM KCLQNENLID KESASLLWNF IVLLCRQNGT VVGTDIAELL
LRDHRTVWLP GKSPNEANLI DFTNEAVEQV EEEESGEAQL SFLTGGPAAA ASSLERETER
FRELLLYGRK KDALESAMKN GLWGHALLLA SKMDSRTHAR VMTRFANSLP INDPLQTVYQ
LMSGRMPAAS TCCGDEKWGD WRPHLAMVLS NLNNNMDVES RTMATMGDTL ASRGLLDAAH
FCYLMAQAGF GVYTKKTTKL VLIGSNHSLP FLKFATNEAI QRTEAYEYAQ SLGAETCPLP
SFQVFKFIYS CRLAEMGLAT QAFHYCEAIA KSILTQPHLY SPVLISQLVQ MASQLRLFDP
QLKEKPEEES LAAPTWLVHL QQVERQIKEG AGVWHQDGAL PQQCPGTPSS EMEQLDRPGL
SQPGALGIAN PLLAVPAPSP EHSSPSVRLL PSAPQTLPDG PLASPARVPM FPVPLPPGPL
EPGPGCVTPG PALGFLEPSG PGLPPGVPPL QERRHLLQEA RSPDPGIVPQ EAPVGNSLSE
LSEENFDGKF ANLTPSRTVP DSEAPPGWDR ADSGPTQPPL SLSPAPETKR PGQAAKKETK
EPKKGESWFF RWLPGKKKTE AYLPDDKNKS IVWDEKKNQW VNLNEPEEEK KAPPPPPTSM
PKTVQAAPPA LPGPPGAPVN MYSRRAAGTR ARYVDVLNPS GTQRSEPALA PADFVAPLAP
LPIPSNLFVP TPDAEEPQLP DGTGREGPAA ARGLANPEPA PEPKVLSSAA SLPGSELPSS
RPEGSQGGEL SRCSSMSSLS REVSQHFNQA PGDLPAAGGP PSGAMPFYNP AQLAQACATS
GSSRLGRIGQ RKHLVLN
