SC31A_MOUSE
ID SC31A_MOUSE Reviewed; 1230 AA.
AC Q3UPL0; Q3UYH3; Q6IQZ3; Q7TQJ7; Q811J4;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Protein transport protein Sec31A;
DE AltName: Full=SEC31-like protein 1;
DE AltName: Full=SEC31-related protein A;
GN Name=Sec31a; Synonyms=Sec31l1;
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 MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 286-1230 (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-612 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata, and Olfactory bulb;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526 AND SER-531, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526 AND SER-531, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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 [7]
RP 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 [8]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-423, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Component of the coat protein complex II (COPII) which
CC promotes the formation of transport vesicles from the endoplasmic
CC reticulum (ER) (By similarity). The coat has two main functions, the
CC physical deformation of the endoplasmic reticulum membrane into
CC vesicles and the selection of cargo molecules (By similarity).
CC {ECO:0000250|UniProtKB:O94979, ECO:0000250|UniProtKB:Q9Z2Q1}.
CC -!- SUBUNIT: COPII is composed of at least 5 proteins: the SEC23/24
CC complex, the SEC13/31 complex and SAR1. SEC13 and SEC31 make a 2:2
CC tetramer that forms the edge element of the COPII outer coat. The
CC tetramer self-assembles in multiple copies to form the complete
CC polyhedral cage. Interacts (via WD 8) with SEC13 (By similarity).
CC Interacts with PDCD6; interaction takes place in response to cytosolic
CC calcium increase and leads to bridge together the BCR(KLHL12) complex
CC and SEC31A, leading to monoubiquitination. Interacts with KLHL12 (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:O94979}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle,
CC COPII-coated vesicle membrane {ECO:0000250|UniProtKB:O94979};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:O94979}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:O94979}. Endoplasmic reticulum membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC Note=Associates with membranes in a GTP-dependent manner (By
CC similarity). Localizes to endoplasmic reticulum exit sites (ERES), also
CC known as transitional endoplasmic reticulum (tER) (PubMed:25201882).
CC {ECO:0000250|UniProtKB:Q9Z2Q1, ECO:0000269|PubMed:25201882}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3UPL0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UPL0-2; Sequence=VSP_026753;
CC Name=3;
CC IsoId=Q3UPL0-3; Sequence=VSP_026752;
CC -!- DOMAIN: The ALG-2-binding site motif-2 (ABS-2) contains a PXPGF
CC sequence that binds hydrophobic pocket 3 of PDCD6.
CC {ECO:0000250|UniProtKB:O94979}.
CC -!- PTM: Monoubiquitinated by the BCR(KLHL12) E3 ubiquitin ligase complex,
CC leading to regulate the size of COPII coats.
CC {ECO:0000250|UniProtKB:O94979}.
CC -!- SIMILARITY: Belongs to the WD repeat SEC31 family. {ECO:0000305}.
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DR EMBL; BC043942; AAH43942.1; -; mRNA.
DR EMBL; BC054358; AAH54358.1; -; mRNA.
DR EMBL; BC071249; AAH71249.1; -; mRNA.
DR EMBL; AK134681; BAE22239.1; -; mRNA.
DR EMBL; AK143455; BAE25385.1; -; mRNA.
DR CCDS; CCDS51573.1; -. [Q3UPL0-1]
DR RefSeq; NP_081245.1; NM_026969.1. [Q3UPL0-1]
DR RefSeq; XP_011247860.1; XM_011249558.2. [Q3UPL0-2]
DR AlphaFoldDB; Q3UPL0; -.
DR SMR; Q3UPL0; -.
DR BioGRID; 213263; 18.
DR IntAct; Q3UPL0; 2.
DR MINT; Q3UPL0; -.
DR STRING; 10090.ENSMUSP00000092157; -.
DR iPTMnet; Q3UPL0; -.
DR PhosphoSitePlus; Q3UPL0; -.
DR SwissPalm; Q3UPL0; -.
DR EPD; Q3UPL0; -.
DR jPOST; Q3UPL0; -.
DR MaxQB; Q3UPL0; -.
DR PaxDb; Q3UPL0; -.
DR PeptideAtlas; Q3UPL0; -.
DR PRIDE; Q3UPL0; -.
DR ProteomicsDB; 256601; -. [Q3UPL0-1]
DR ProteomicsDB; 256602; -. [Q3UPL0-2]
DR ProteomicsDB; 256603; -. [Q3UPL0-3]
DR Antibodypedia; 1692; 150 antibodies from 23 providers.
DR Ensembl; ENSMUST00000094578; ENSMUSP00000092157; ENSMUSG00000035325. [Q3UPL0-1]
DR Ensembl; ENSMUST00000182886; ENSMUSP00000138213; ENSMUSG00000035325. [Q3UPL0-2]
DR GeneID; 69162; -.
DR KEGG; mmu:69162; -.
DR UCSC; uc008yhi.1; mouse. [Q3UPL0-2]
DR UCSC; uc008yhk.2; mouse. [Q3UPL0-1]
DR CTD; 22872; -.
DR MGI; MGI:1916412; Sec31a.
DR VEuPathDB; HostDB:ENSMUSG00000035325; -.
DR eggNOG; KOG0307; Eukaryota.
DR GeneTree; ENSGT00390000003175; -.
DR HOGENOM; CLU_003033_1_0_1; -.
DR InParanoid; Q3UPL0; -.
DR OMA; NRYAPAP; -.
DR OrthoDB; 100998at2759; -.
DR PhylomeDB; Q3UPL0; -.
DR TreeFam; TF313842; -.
DR Reactome; R-MMU-204005; COPII-mediated vesicle transport.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR BioGRID-ORCS; 69162; 12 hits in 75 CRISPR screens.
DR ChiTaRS; Sec31a; mouse.
DR PRO; PR:Q3UPL0; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q3UPL0; protein.
DR Bgee; ENSMUSG00000035325; Expressed in vault of skull and 259 other tissues.
DR ExpressionAtlas; Q3UPL0; baseline and differential.
DR Genevisible; Q3UPL0; MM.
DR GO; GO:0030127; C:COPII vesicle coat; ISS:UniProtKB.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0030120; C:vesicle coat; ISO:MGI.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
DR GO; GO:0005198; F:structural molecule activity; IBA:GO_Central.
DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; ISO:MGI.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0051592; P:response to calcium ion; ISO:MGI.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR024298; ACE1_Sec16_Sec31.
DR InterPro; IPR040251; SEC31-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR13923; PTHR13923; 1.
DR Pfam; PF12931; Sec16_C; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoplasmic vesicle;
KW Endoplasmic reticulum; ER-Golgi transport; Isopeptide bond; Membrane;
KW Methylation; Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW Transport; Ubl conjugation; WD repeat.
FT CHAIN 1..1230
FT /note="Protein transport protein Sec31A"
FT /id="PRO_0000295148"
FT REPEAT 4..47
FT /note="WD 1"
FT REPEAT 64..111
FT /note="WD 2"
FT REPEAT 120..160
FT /note="WD 3"
FT REPEAT 166..206
FT /note="WD 4"
FT REPEAT 209..254
FT /note="WD 5"
FT REPEAT 258..298
FT /note="WD 6"
FT REPEAT 301..342
FT /note="WD 7"
FT REPEAT 397..429
FT /note="WD 8; interaction with SEC13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REGION 161..470
FT /note="Interaction with SEC13"
FT /evidence="ECO:0000250|UniProtKB:O94979"
FT REGION 789..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 799..1123
FT /note="Interaction with PDCD6"
FT /evidence="ECO:0000250|UniProtKB:O94979"
FT REGION 924..1104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 841..847
FT /note="ALG-2-binding site motif-2 (ABS-2),"
FT /evidence="ECO:0000250|UniProtKB:O94979"
FT COMPBIAS 792..806
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..876
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..947
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..1001
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1035..1065
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1090
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 423
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 526
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 531
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18630941,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 798
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94979"
FT MOD_RES 1171
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O94979"
FT MOD_RES 1173
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94979"
FT CROSSLNK 646
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O94979"
FT CROSSLNK 1227
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O94979"
FT VAR_SEQ 1..923
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026752"
FT VAR_SEQ 503..541
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026753"
FT CONFLICT 820
FT /note="S -> P (in Ref. 1; AAH54358)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1230 AA; 133569 MW; B6119EFDEF121A76 CRC64;
MKLKEIDRTA MQAWSPAQNH PIYLATGTSA QQLDATFSTN ASLEIFELDL SDPSLDMKSC
ATFSSSHRYH KLIWGPHKMD SKGDVSGVLI AGGENGNIIL YDPSKIIAGD KEVVIAQKDK
HTGPVRALDV NIFQTNLVAS GANESEIYIW DLNNFATPMT PGAKTQPPED ISCIAWNRQV
QHILASASPS GRATVWDLRK NEPIIKVSDH SNRMHCSGLA WHPDVATQMV LASEDDRLPV
IQMWDLRFAS SPLRVLENHA RGILAVAWSM ADPELLLSCG KDAKILCSNP NTGEVLYELP
TNTQWCFDIQ WCPRNPAVLS AASFDGRISV YSIMGGSIDG LRQKQVDKLS SSFGNLDPFG
TGQPLPPLQI PQQSAQHSIV LPLKKPPKWI RRPVGASFSF GGKLVTFESV AVPLQQGAEQ
QRRQPVFISQ VVTEKDFLNR SAQLQHAVQS QGFIGYCQKK IEASQTEFEK NVWSFLKVNF
EEDSRGKYLE LLGYRKEDLG QKIALALNKV DGPDVALKDS DQVAQSDGEE SPAAEEQLLG
ERIKEEKQEC DFLPSAGGTF NISVSGDIDG LITRALLTGN FESAVDLCLH DNRMADAIIL
AIAGGQELLA QTQKKYFAKS QSKITRLITA VVMKNWREIV ESCDLKNWRE ALAAVLTYAK
PDEFSALCDL LGTRLEREGD SLLRTQACLC YICAGNVERL VACWTKAQDG SSPLSLQDLI
EKVVILRKAV QLTQALDTNT VGALLAEKMS QYASLLAAQG SIAAALAFLP DNTNQPNIVQ
LRDRLCKAQG KPVSGQESSQ SPYERQPLSK GRPGPVAGHS QMPRVQTQQY YPHGENPPPP
GFIMQGNVIP NPAAPLPTAP GHMPSQLPPY PQPQPYQPAQ QYSFGTGGAA AYRPQQPVAP
PASNAYPNTP YISPVASYSG QPQMYTAQQA SSPTSSSAAS FPPPSSGASF QHGGPGAPPS
SSAYALPPGT TGTPPAASEL PASQRTENQS FQDQASILEG PQNGWNDPPA LNRVPKKKKM
PENFMPPVPI TSPIMNPSGD PQSQGLQQQP STPGPLSSHA SFPQQHLAGG QPFHGVQQPL
AQTGMPPSFS KPNTEGAPGA PIGNTIQHVQ ALPTEKITKK PIPEEHLILK TTFEDLIQRC
LSSATDPQTK RKLDDASKRL EFLYDKLREQ TLSPTIINGL HSIARSIETR NYSEGLSVHT
HIVSTSNFSE TSAFMPVLKV VLSQASKLGV
