SC16A_MOUSE
ID SC16A_MOUSE Reviewed; 2357 AA.
AC E9QAT4; A2AIX1; Q80U43; Q811L5;
DT 07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 73.
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;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1426-2357 (ISOFORM 2).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1452-2357 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP FUNCTION, AND INTERACTION WITH SEC23A.
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP INTERACTION WITH LRRK2, 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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RAB10.
RX PubMed=27354378; DOI=10.1083/jcb.201509052;
RA Bruno J., Brumfield A., Chaudhary N., Iaea D., McGraw T.E.;
RT "SEC16A is a RAB10 effector required for insulin-stimulated GLUT4
RT trafficking in adipocytes.";
RL J. Cell Biol. 214:61-76(2016).
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:17428803).
CC Mediates the recruitment of MIA3/TANGO to ERES. Regulates both
CC conventional (ER/Golgi-dependent) and GORASP2-mediated unconventional
CC (ER/Golgi-independent) trafficking of CFTR to cell membrane (By
CC similarity). Acts as a RAB10 effector in the regulation of insulin-
CC induced SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to
CC the plasma membrane in adipocytes (PubMed:27354378).
CC {ECO:0000250|UniProtKB:O15027, ECO:0000269|PubMed:17428803,
CC ECO:0000269|PubMed:27354378}.
CC -!- SUBUNIT: SEC16A and SEC16B are each present in multiple copies in a
CC heteromeric complex (By similarity). Interacts with SEC23A
CC (PubMed:17428803). Interacts with RNF183, RNF152, MIA3 and SEC13 (By
CC similarity). Interacts with GORASP2 in response to ER stress (By
CC similarity). Interacts with LRRK2 (via ROC domain) (PubMed:25201882).
CC Interacts with RAB10 (PubMed:27354378). {ECO:0000250|UniProtKB:O15027,
CC ECO:0000269|PubMed:17428803, ECO:0000269|PubMed:25201882,
CC ECO:0000269|PubMed:27354378}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O15027}; Peripheral membrane protein. Golgi
CC apparatus membrane {ECO:0000250|UniProtKB:O15027}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:O15027}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:27354378}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:O15027}. Microsome membrane
CC {ECO:0000250|UniProtKB:O15027}. Note=SAR1A activity is required to
CC maintain SEC16A localization at discrete locations on the ER membrane
CC perhaps by preventing its dissociation (By similarity). 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). Recruited to microsomal
CC membrane in SAR1-dependent manner (By similarity).
CC {ECO:0000250|UniProtKB:O15027, ECO:0000269|PubMed:25201882}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=E9QAT4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=E9QAT4-2; Sequence=VSP_059936;
CC -!- SIMILARITY: Belongs to the SEC16 family. {ECO:0000305}.
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DR EMBL; AL732541; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC042603; AAH42603.1; -; mRNA.
DR EMBL; AK122242; BAC65524.3; -; mRNA.
DR CCDS; CCDS38085.1; -. [E9QAT4-1]
DR RefSeq; NP_694765.2; NM_153125.2. [E9QAT4-1]
DR RefSeq; XP_006497974.1; XM_006497911.3. [E9QAT4-2]
DR AlphaFoldDB; E9QAT4; -.
DR IntAct; E9QAT4; 8.
DR MINT; E9QAT4; -.
DR STRING; 10090.ENSMUSP00000109716; -.
DR iPTMnet; E9QAT4; -.
DR PhosphoSitePlus; E9QAT4; -.
DR EPD; E9QAT4; -.
DR jPOST; E9QAT4; -.
DR MaxQB; E9QAT4; -.
DR PaxDb; E9QAT4; -.
DR PeptideAtlas; E9QAT4; -.
DR PRIDE; E9QAT4; -.
DR ProteomicsDB; 311996; -.
DR ProteomicsDB; 361542; -. [E9QAT4-1]
DR Antibodypedia; 1693; 54 antibodies from 19 providers.
DR DNASU; 227648; -.
DR Ensembl; ENSMUST00000091252; ENSMUSP00000088796; ENSMUSG00000026924. [E9QAT4-1]
DR Ensembl; ENSMUST00000114082; ENSMUSP00000109716; ENSMUSG00000026924. [E9QAT4-2]
DR GeneID; 227648; -.
DR KEGG; mmu:227648; -.
DR UCSC; uc008ivi.1; mouse. [E9QAT4-1]
DR CTD; 9919; -.
DR MGI; MGI:2139207; Sec16a.
DR VEuPathDB; HostDB:ENSMUSG00000026924; -.
DR eggNOG; KOG1913; Eukaryota.
DR GeneTree; ENSGT00940000159324; -.
DR HOGENOM; CLU_001465_0_0_1; -.
DR OMA; LERWKGA; -.
DR OrthoDB; 235062at2759; -.
DR TreeFam; TF316276; -.
DR Reactome; R-MMU-204005; COPII-mediated vesicle transport.
DR BioGRID-ORCS; 227648; 13 hits in 74 CRISPR screens.
DR ChiTaRS; Sec16a; mouse.
DR PRO; PR:E9QAT4; -.
DR Proteomes; UP000000589; Chromosome 2.
DR Bgee; ENSMUSG00000026924; Expressed in animal zygote and 245 other tissues.
DR ExpressionAtlas; E9QAT4; baseline and differential.
DR Genevisible; E9QAT4; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
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; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA: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; IMP:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISO:MGI.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0043000; P:Golgi to plasma membrane CFTR protein transport; ISS: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; ISS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS: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_0000445696"
FT REGION 1..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 917..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1023..1055
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1037..1905
FT /note="Required for localization to endoplasmic reticulum
FT exit sites"
FT /evidence="ECO:0000250|UniProtKB:O15027"
FT REGION 1076..1151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1118..1415
FT /note="Interaction with MIA3"
FT /evidence="ECO:0000250|UniProtKB:O15027"
FT REGION 1119..1420
FT /note="Required for endoplasmic reticulum localization"
FT /evidence="ECO:0000250|UniProtKB:O15027"
FT REGION 1226..1253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1344..1395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1449..1905
FT /note="Central conserved domain (CCD); mediates interaction
FT with RNF183, LRRK2 and SEC13"
FT /evidence="ECO:0000250|UniProtKB:O15027"
FT REGION 1907..1943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1993..2141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2126..2357
FT /note="Required for interaction with SEC23A"
FT /evidence="ECO:0000250|UniProtKB:O15027"
FT REGION 2156..2198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2240..2357
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 53..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..613
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..811
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..964
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 973..1008
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1103
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1344..1371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1372..1395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2074..2108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2110..2141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2156..2172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2173..2191
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2268..2287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2330..2346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15027"
FT MOD_RES 581
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15027"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15027"
FT MOD_RES 609
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15027"
FT MOD_RES 611
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15027"
FT MOD_RES 614
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15027"
FT MOD_RES 615
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O15027"
FT MOD_RES 617
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15027"
FT MOD_RES 1087
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15027"
FT MOD_RES 1223
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15027"
FT MOD_RES 1245
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15027"
FT MOD_RES 1340
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O15027"
FT MOD_RES 1342
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15027"
FT MOD_RES 1362
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15027"
FT MOD_RES 1365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15027"
FT MOD_RES 1371
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15027"
FT MOD_RES 1374
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15027"
FT MOD_RES 1377
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15027"
FT MOD_RES 1384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15027"
FT MOD_RES 1588
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15027"
FT MOD_RES 1616
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15027"
FT MOD_RES 1922
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O15027"
FT MOD_RES 1951
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15027"
FT MOD_RES 2043
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15027"
FT MOD_RES 2063
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15027"
FT MOD_RES 2077
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15027"
FT MOD_RES 2094
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15027"
FT MOD_RES 2291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15027"
FT VAR_SEQ 2309
FT /note="E -> ELSRCSSLSSLSQEVSRHFHQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_059936"
FT CONFLICT 2038
FT /note="P -> L (in Ref. 2; AAH42603)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2357 AA; 254202 MW; BF482E74AEFD7157 CRC64;
MQPPPQAVPS GVAGPPPAGN PRSMFWANSP YRKPANNAPV APITRPLQPV TDPFAFNRQT
LQNTPVGSSS KSSLPNLPGP ALSVFSQWPG LPVTPTNAGD SSTGLHEPLS GTLSQPRADA
SLFPPASTPS SLPGLEVSRN AEADPSSGHE VQMLPHSAHY IPGVGPEQPL GGQMNDSGSG
PDQPMNRHAP HDGAVTHAAS PFLPQPQMPG QWGPAQGGPQ PSYQHHSPYL EGPVQNMGLQ
AASLPHFPPP SSLHQGPGHE SHAPQTFTPA SLASGEGNEI VHQQSKNHPL SSFPPKHTFE
QNSRIGNMWA SPELKQNPGV NKEHLLDPAH VNPFTQGNSP ENQAHHPPVA ATNHALQEAA
SGALSMFFQG EETENEENLS SEKAGLDKRL NLDSFSSTSR LGHPPPPGAS GVYQAFPRGP
SSEAAQEGDA QPYFSQSVGV RLDKQSTVPP ANDAWGDVPG TGTRCASGPQ CENVENLEFV
QNQEVLPRET LSVDPFPLSD QIRYGPLPGP AASRPATVGL TRGGGLNLEA PDTPLHPTRP
DSVSSSYSSH SHRSPPGSAR PQELVGTFIQ QEVGKLEDDT SGSFFKQIDS SPVGGETDEV
TGSQNCCSSL SQPSTPSPPK PTGVFQTSAN SSFEPVKSHL VGVKPVEADR ANMVVEVRGT
QYCPKKRRAA VAPPDATSGN LEQPPDNMET PCAPQACPLP LSTTGEAGQL VSNTAGTPLD
TVRPVPDKRP SARAQGPVKC ESPATTLWAQ NELPDFGGNV LLAPAAPALY VPVKPKPSEV
VHHPEKGMSG QKAWKQGSVP PLQNQDPPGA SENLENPPKV GEEEALPVQA SSGYASLLSS
PPTESLHNQP VLIAQPDQSY NLAQPINFSV SLLNPNEKNQ SWGDAVVGER SIVSNNWALG
GDPEERAALS GVPASAVTGA SLPSSIPQNC APQGSGSSEM IASQSASWLV QQLSPQTPQS
PHPNAEKGPS EFVSSPAGNT SVMLVPPASS TLVPNSNKAK HSSNQEEAVG ALDFTLNRTL
ENPVRMYSPS PSDGPASQQP LPNHPRQSGP GLHNQDHFYQ QVTKDAQDQH RLERAQPELV
PPRPQNSPQV PQASCPEPSN PESPPTQGQS ESLAQPPASP ASVNTGQLLP QPPQASSASV
TSTNSSQAAV RSEQLWLHPP PPNTFGPAPQ DLASYYYYRP LYDAYQSQYP SPYPSDPGTA
SLYYQDMYGL YEPRYRPYDS SASAYAENHR YSEPERPSSR ASHYSDQLAP RQGYPEGYYN
SKSGWSSHSD YYANYYSGQY DYGDPSRWDR YYGSRLRDPR TWDRRYWYDS EHDPYRKDHY
AYSDRPEKCD DHWRYDPRFT GSFDDDAEIH RDPYGEEADR RSIHSEHSAR SLRSTHSLPS
RRSSLSSHSH QSQIYRSHHV TGGSFEAPHA PGSFHGDYAY GTYASNFSGA HGFPEYSYPA
DTSWPAVEQV PSRPTSPEKF TVPHVCARFG PGGQLLKVIP NLPSEGQPAL VEIHSLETLL
QHTPEQEEMR SFPGPLGKDD THKVDVINFA QNKATKCLQN ESLIDKESAS LLWKFIILLC
RQNGTVVGTD IAELLLRDHR TVWLPGKSPN EANLIDFTNE AVEQVEEEES GEAQLSFLTD
SQTVTTSVLE KETERFRELL LYGRKKDALE SAMKNGLWGH ALLLASKMDS RTHARVMTRF
ANSLPINDPL QTVYQLMSGR MPAASTCCGD EKWGDWRPHL AMVLSNLNNN MDVESRTMAT
MGDTLASKGL LDAAHFCYLM AQVGFGVYTK KTTKLVLIGS NHSLPFLKFA TNEAIQRTEA
YEYAQSLGAH TCSLPNFQVF KFIYLCRLAE MGLATQAFHY CEVIAKSVLT QPGAYSPVLI
SQLTQMASQL RLFDPQLKEK PEEESFVEPA WLVQLQHVER QIQEGTVLWS QDGTEPQQCR
ITSGSEVEQS DGPGLNQQAG PQADNPLLMP STEPLMHGVQ LLPTAPQTLP DGQPAHLSRV
PMFPVPMSRG PLELSPAYGP PGSALGFPES SRSDPAVLHP GQALPPTTLS LQESGLPPQE
AKSPDPEMVP RGSPVRHSPP ELSQEEFGES FADPGSSRTA QDLETSPVWD LGSSSLTRAP
SLTSDSEGKK PAQAVKKEPK EPKKTESWFS RWLPGKKRTE AYLPDDKNKS IVWDEKKNQW
VNLNEPEEEK KAPPPPPTSF PRVPQVAPTG PAGPPTASVN VFSRKAGGSR ARYVDVLNPS
GTQRSEPALA PADFFAPLAP LPIPSNLFVP NPDAEEPQPA DGTGCRGQAP AGTQSKAEST
LEPKVGSSTV SAPGPELLPS KPDGSQGGEA PGDHCPTGAP HGGSVPFYNP AQLVQASVTS
GNSRPGRIGQ RKYAALN
