SNED1_RAT
ID SNED1_RAT Reviewed; 1403 AA.
AC Q5ZQU0; Q336F3;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Sushi, nidogen and EGF-like domain-containing protein 1 {ECO:0000305};
DE AltName: Full=Insulin-responsive sequence DNA-binding protein 1 {ECO:0000303|PubMed:15194686};
DE Short=IRE-BP1 {ECO:0000303|PubMed:15194686};
DE Flags: Precursor;
GN Name=Sned1 {ECO:0000312|RGD:1566079};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 396-1403, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=15194686; DOI=10.1074/jbc.m404349200;
RA Villafuerte B.C., Phillips L.S., Rane M.J., Zhao W.;
RT "Insulin-response element-binding protein 1: a novel Akt substrate involved
RT in transcriptional action of insulin.";
RL J. Biol. Chem. 279:36650-36659(2004).
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:Q70E20}. Note=Forms microfibrils within
CC the extracellular matrix and colocalizes with fibronectin (FN1).
CC {ECO:0000250|UniProtKB:Q70E20}.
CC -!- TISSUE SPECIFICITY: Expressed in liver. {ECO:0000269|PubMed:15194686}.
CC -!- PTM: Phosphorylated on serine and threonine residues.
CC {ECO:0000250|UniProtKB:Q8TER0}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8TER0}.
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DR EMBL; AABR03068156; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03069106; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03069488; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03071665; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03072503; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF439715; AAQ04556.1; -; mRNA.
DR EMBL; AF439719; AAQ04601.1; -; mRNA.
DR RefSeq; XP_006245588.1; XM_006245526.3.
DR AlphaFoldDB; Q5ZQU0; -.
DR SMR; Q5ZQU0; -.
DR STRING; 10116.ENSRNOP00000022290; -.
DR GlyGen; Q5ZQU0; 3 sites.
DR iPTMnet; Q5ZQU0; -.
DR PhosphoSitePlus; Q5ZQU0; -.
DR PaxDb; Q5ZQU0; -.
DR Ensembl; ENSRNOT00000022290; ENSRNOP00000022290; ENSRNOG00000023548.
DR GeneID; 316638; -.
DR UCSC; RGD:1566079; rat.
DR CTD; 25992; -.
DR RGD; 1566079; Sned1.
DR eggNOG; KOG1217; Eukaryota.
DR eggNOG; KOG4291; Eukaryota.
DR GeneTree; ENSGT00940000160730; -.
DR InParanoid; Q5ZQU0; -.
DR OrthoDB; 7525at2759; -.
DR PhylomeDB; Q5ZQU0; -.
DR PRO; PR:Q5ZQU0; -.
DR Proteomes; UP000002494; Chromosome 9.
DR GO; GO:0031012; C:extracellular matrix; ISO:RGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005112; F:Notch binding; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR CDD; cd00033; CCP; 1.
DR CDD; cd00063; FN3; 3.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003886; NIDO_dom.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR Pfam; PF00008; EGF; 13.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF06119; NIDO; 1.
DR SMART; SM00032; CCP; 1.
DR SMART; SM00181; EGF; 15.
DR SMART; SM00179; EGF_CA; 14.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00539; NIDO; 1.
DR SUPFAM; SSF49265; SSF49265; 2.
DR SUPFAM; SSF57184; SSF57184; 1.
DR SUPFAM; SSF57535; SSF57535; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 6.
DR PROSITE; PS00022; EGF_1; 15.
DR PROSITE; PS01186; EGF_2; 14.
DR PROSITE; PS50026; EGF_3; 15.
DR PROSITE; PS01187; EGF_CA; 3.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS51220; NIDO; 1.
DR PROSITE; PS50923; SUSHI; 1.
PE 2: Evidence at transcript level;
KW Calcium; Disulfide bond; EGF-like domain; Extracellular matrix;
KW Glycoprotein; Phosphoprotein; Reference proteome; Repeat; Secreted; Signal;
KW Sushi.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1403
FT /note="Sushi, nidogen and EGF-like domain-containing
FT protein 1"
FT /id="PRO_0000299555"
FT DOMAIN 103..258
FT /note="NIDO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00570"
FT DOMAIN 268..309
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 311..347
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 349..385
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 387..423
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 429..465
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 468..500
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 541..577
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 580..616
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 619..655
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 657..693
FT /note="EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 696..753
FT /note="Sushi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 753..789
FT /note="EGF-like 11; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 791..827
FT /note="EGF-like 12; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 829..865
FT /note="EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 867..903
FT /note="EGF-like 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 908..1006
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1007..1105
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1106..1200
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1306..1342
FT /note="EGF-like 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 1295..1314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 712
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 886
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 977
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1015
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 272..284
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 278..297
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 299..308
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 315..326
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 320..335
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 337..346
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 353..364
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 358..373
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 375..384
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 391..402
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 396..411
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 413..422
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 433..444
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 438..453
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 455..464
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 472..480
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 474..488
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 490..499
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 545..556
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 550..565
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 567..576
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 584..595
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 589..604
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 606..615
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 623..634
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 628..643
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 645..654
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 661..672
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 666..681
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 683..692
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 698..739
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 724..751
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 757..768
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 762..777
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 779..788
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 795..806
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 800..815
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 817..826
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 833..844
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 838..853
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 855..864
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 871..882
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 876..891
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 893..902
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1310..1321
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1315..1330
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1332..1341
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CONFLICT 494
FT /note="F -> S (in Ref. 1; AAQ04556)"
FT /evidence="ECO:0000305"
FT CONFLICT 595
FT /note="C -> Y (in Ref. 1; AAQ04556)"
FT /evidence="ECO:0000305"
FT CONFLICT 762
FT /note="C -> Y (in Ref. 1; AAQ04556)"
FT /evidence="ECO:0000305"
FT CONFLICT 826
FT /note="C -> Y (in Ref. 1; AAQ04556)"
FT /evidence="ECO:0000305"
FT CONFLICT 869
FT /note="D -> N (in Ref. 1; AAQ04556)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1403 AA; 151401 MW; 7E1C2788103D7E19 CRC64;
MRRGAAWALL LAAALGLGAR GVRAAVALAD FYPFGTKRGD AVTPKQDDGG SGLQPLSVPF
PFFGAEHSGL YVNNNGIISF LKEVSQFTPV AFPIAKDRCV VAAFWADVDN RRAGDVYYRE
ATDAAMLNRA TEDIRRYFPE LPDFSATWVF VATWYRVTFF GGSSSSPVNT FQTVLITDGR
FSFTIFNYES ILWTTGTHAS SGGDADGLGG IAAQAGFNAG DGHRYFNIPG SRTADMAEVE
TTTNVGVPGR WAFRIDDAQV RVGGCGHTTS VCLVLRPCLN GGKCIDDCVT GNPSYTCSCL
AGFTGRRCHL DVNECASHPC QNGGTCTHGV NSFSCQCPAG FQGPTCESAQ SPCDNKVCQN
GGQCQAESSS AVCVCQAGYT GATCETDVDE CSSDPCLNGG SCVDLVGNYS CICVEPFEGP
QCETGSYVVP SPCLSNPCLN GGTCVDADQG YVCECPEGFM GLDCRERILN DCDCRNGGRC
LGANTTICQC PPGFFGLLCE FEVTATPCNM NTQCPDGGYC MEYGGSYLCV CHTDHNISHS
LPSPCDSDPC FNGGSCDAHE DSYTCECPRG FHGRHCEKAR PHLCSSGPCR NGGTCKETGD
EYRCTCPYRF TGRHCEIGKP DSCASGPCHN GGTCFHYIGK YKCDCPPGFS GRHCEIAPSP
CFRSPCMNGG ICEDLGTDFS CHCQPGYTGH RCQAEVDCGQ PEEVKHATMR LNGTRMGSVA
LYTCDPGFSL SVLSHMRVCQ PQGVWSQPPQ CIEVDECQSQ PCLHKGSCQD LIAGYQCLCS
PGYEGVHCEL ETDECQAQPC RNGGSCRDLP GAFICQCPEG FVGTHCETEV DACASSPCQH
GGRCEDGGGA YLCVCPEGFF GYNCETVSDP CFSSPCGGRG YCLASNGSHS CTCKVGYTGK
DCTKELLPPT ALRVERVEES GVSISWSPPE GTTARQVLDG YAVTYASSDG SSRRTDFVDR
SRSSHQLRAL AAGRAYNISV FSVKRNTNNK NDISRPAALL TRTRPRPIED FEVTNISANA
ISVQWALHRI QHATVSRVRV SVLYPEDTVV QSTEVDRSVD RLTFGDLLPG RRYSVRLTTL
SGPGGAEYPT ESLASAPLNV WTRPLPPANL TASRVTATSA HMVWDPPTPG ISLEAYVINV
TTSQNTKSRY IPNGKLVSYT VRDLMPGRRY QLSVTAVQST EQGQLHSEPA HLYIITSPRD
GTDRRWHQGG HHSRMLRNRP APLRLPELRL LNDHGAPETP TQPPRFSELV DGRARVSARF
GGLPSRAVTV RSQPTTPVPL KNTEAPEQAR LALQLPKNNS KDTESTPGSC SEDTCQNGGT
CVPGANAHSC DCRPGFKGRH CELACEKVPR PCTRLFSETK SFPVWEGDVC HHVYKKVYKV
HQDVCFKERC QSTSLKKLKQ ESN
