SBNO1_HUMAN
ID SBNO1_HUMAN Reviewed; 1393 AA.
AC A3KN83; Q05C06; Q3ZTS3; Q9H3T8; Q9NVB2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Protein strawberry notch homolog 1;
DE AltName: Full=Monocyte protein 3;
DE Short=MOP-3;
GN Name=SBNO1; Synonyms=MOP3;
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 [MRNA] (ISOFORM 2).
RC TISSUE=Blood;
RA Takayama K., Ukai Y., Fujii Y., Yoshimoto M.;
RT "Molecular and biological characterization of a new nuclear protein, MOP-3
RT which is highly expressed in human monocytes.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-793 (ISOFORM 3).
RC TISSUE=Placenta;
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 1-783 (ISOFORM 2).
RC TISSUE=Teratocarcinoma;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-1393 (ISOFORM 4).
RX PubMed=16533400; DOI=10.1186/1471-2164-7-48;
RA Kemmer D., Podowski R.M., Arenillas D., Lim J., Hodges E., Roth P.,
RA Sonnhammer E.L.L., Hoeoeg C., Wasserman W.W.;
RT "NovelFam3000 -- uncharacterized human protein domains conserved across
RT model organisms.";
RL BMC Genomics 7:48-48(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-697, AND IDENTIFICATION BY
RP 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214 AND SER-794, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-794 AND SER-815, AND
RP 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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-149; LYS-413 AND LYS-1222, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-754; SER-755 AND SER-794, AND
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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-754 AND SER-755, AND
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148; SER-162; SER-794 AND
RP SER-1386, 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 [13]
RP VARIANTS [LARGE SCALE ANALYSIS] SER-634; LYS-889 AND CYS-997.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=A3KN83-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A3KN83-2; Sequence=VSP_030296;
CC Name=3;
CC IsoId=A3KN83-3; Sequence=VSP_030295;
CC Name=4;
CC IsoId=A3KN83-4; Sequence=VSP_030296, VSP_030297, VSP_030298;
CC -!- SIMILARITY: Belongs to the SBNO family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ76814.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB014772; BAB19784.1; -; mRNA.
DR EMBL; BC030544; AAH30544.1; -; mRNA.
DR EMBL; BC133704; AAI33705.1; -; mRNA.
DR EMBL; AK001695; BAA91842.1; -; mRNA.
DR EMBL; AY364255; AAQ76814.1; ALT_INIT; mRNA.
DR CCDS; CCDS53844.1; -. [A3KN83-1]
DR CCDS; CCDS9246.1; -. [A3KN83-2]
DR RefSeq; NP_001161328.1; NM_001167856.2. [A3KN83-1]
DR RefSeq; NP_060653.3; NM_018183.4. [A3KN83-2]
DR RefSeq; XP_005253630.1; XM_005253573.4.
DR RefSeq; XP_005253633.1; XM_005253576.3.
DR RefSeq; XP_006719536.1; XM_006719473.3.
DR RefSeq; XP_006719537.1; XM_006719474.3.
DR RefSeq; XP_011536835.1; XM_011538533.2.
DR RefSeq; XP_016875045.1; XM_017019556.1.
DR AlphaFoldDB; A3KN83; -.
DR BioGRID; 120502; 57.
DR IntAct; A3KN83; 7.
DR STRING; 9606.ENSP00000387361; -.
DR GlyConnect; 2874; 1 O-Linked glycan (1 site).
DR GlyGen; A3KN83; 10 sites, 2 O-linked glycans (10 sites).
DR iPTMnet; A3KN83; -.
DR MetOSite; A3KN83; -.
DR PhosphoSitePlus; A3KN83; -.
DR BioMuta; SBNO1; -.
DR EPD; A3KN83; -.
DR jPOST; A3KN83; -.
DR MassIVE; A3KN83; -.
DR MaxQB; A3KN83; -.
DR PaxDb; A3KN83; -.
DR PeptideAtlas; A3KN83; -.
DR PRIDE; A3KN83; -.
DR ProteomicsDB; 582; -. [A3KN83-1]
DR ProteomicsDB; 583; -. [A3KN83-2]
DR ProteomicsDB; 584; -. [A3KN83-3]
DR ProteomicsDB; 585; -. [A3KN83-4]
DR Antibodypedia; 52514; 25 antibodies from 14 providers.
DR DNASU; 55206; -.
DR Ensembl; ENST00000267176.8; ENSP00000267176.4; ENSG00000139697.14. [A3KN83-2]
DR Ensembl; ENST00000420886.6; ENSP00000387361.2; ENSG00000139697.14. [A3KN83-1]
DR Ensembl; ENST00000602398.3; ENSP00000473665.1; ENSG00000139697.14. [A3KN83-1]
DR GeneID; 55206; -.
DR KEGG; hsa:55206; -.
DR MANE-Select; ENST00000602398.3; ENSP00000473665.1; NM_001167856.3; NP_001161328.1.
DR UCSC; uc010tao.3; human. [A3KN83-1]
DR CTD; 55206; -.
DR DisGeNET; 55206; -.
DR GeneCards; SBNO1; -.
DR HGNC; HGNC:22973; SBNO1.
DR HPA; ENSG00000139697; Tissue enhanced (testis).
DR neXtProt; NX_A3KN83; -.
DR OpenTargets; ENSG00000139697; -.
DR PharmGKB; PA134967986; -.
DR VEuPathDB; HostDB:ENSG00000139697; -.
DR eggNOG; KOG1513; Eukaryota.
DR GeneTree; ENSGT00940000155449; -.
DR HOGENOM; CLU_000212_2_2_1; -.
DR InParanoid; A3KN83; -.
DR OMA; QWFGQDY; -.
DR OrthoDB; 141580at2759; -.
DR PhylomeDB; A3KN83; -.
DR TreeFam; TF313526; -.
DR PathwayCommons; A3KN83; -.
DR SignaLink; A3KN83; -.
DR BioGRID-ORCS; 55206; 682 hits in 1088 CRISPR screens.
DR ChiTaRS; SBNO1; human.
DR GenomeRNAi; 55206; -.
DR Pharos; A3KN83; Tdark.
DR PRO; PR:A3KN83; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; A3KN83; protein.
DR Bgee; ENSG00000139697; Expressed in postcentral gyrus and 196 other tissues.
DR Genevisible; A3KN83; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0048583; P:regulation of response to stimulus; IEA:UniProt.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR026937; SBNO_Helicase_C_dom.
DR InterPro; IPR026741; SNO.
DR InterPro; IPR039187; SNO_AAA.
DR PANTHER; PTHR12706; PTHR12706; 1.
DR Pfam; PF13872; AAA_34; 1.
DR Pfam; PF13871; Helicase_C_4; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1393
FT /note="Protein strawberry notch homolog 1"
FT /id="PRO_0000314555"
FT REGION 129..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 843..870
FT /evidence="ECO:0000255"
FT COMPBIAS 698..721
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..840
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 149
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 413
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 692
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q689Z5"
FT MOD_RES 693
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q689Z5"
FT MOD_RES 697
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 754
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 755
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 768
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q689Z5"
FT MOD_RES 794
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 815
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1222
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1386
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 78..79
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030295"
FT VAR_SEQ 80..81
FT /note="QQ -> Q (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:16533400, ECO:0000303|Ref.1"
FT /id="VSP_030296"
FT VAR_SEQ 722..733
FT /note="VGGLTGSSSDDS -> MSLMRMMKMIPG (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16533400"
FT /id="VSP_030297"
FT VAR_SEQ 734..1393
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16533400"
FT /id="VSP_030298"
FT VARIANT 634
FT /note="T -> S (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_037910"
FT VARIANT 728
FT /note="S -> N (in dbSNP:rs1060105)"
FT /id="VAR_037911"
FT VARIANT 729
FT /note="S -> N (in dbSNP:rs1060105)"
FT /id="VAR_057794"
FT VARIANT 889
FT /note="E -> K (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_037912"
FT VARIANT 997
FT /note="S -> C (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_037913"
FT CONFLICT 4
FT /note="P -> Q (in Ref. 4; AAQ76814)"
FT /evidence="ECO:0000305"
FT CONFLICT 14
FT /note="S -> R (in Ref. 3; BAA91842)"
FT /evidence="ECO:0000305"
FT CONFLICT 555
FT /note="V -> A (in Ref. 4; AAQ76814)"
FT /evidence="ECO:0000305"
FT CONFLICT 774
FT /note="N -> S (in Ref. 1; BAB19784)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1393 AA; 154312 MW; D2C42F29C7EEC20D CRC64;
MVEPGQDLLL AALSESGISP NDLFDIDGGD AGLATPMPTP SVQQSVPLSA LELGLETEAA
VPVKQEPETV PTPALLNVRQ QPPSTTTFVL NQINHLPPLG STIVMTKTPP VTTNRQTITL
TKFIQTTAST RPSVSAPTVR NAMTSAPSKD QVQLKDLLKN NSLNELMKLK PPANIAQPVA
TAATDVSNGT VKKESSNKEG ARMWINDMKM RSFSPTMKVP VVKEDDEPEE EDEEEMGHAE
TYAEYMPIKL KIGLRHPDAV VETSSLSSVT PPDVWYKTSI SEETIDNGWL SALQLEAITY
AAQQHETFLP NGDRAGFLIG DGAGVGKGRT IAGIIYENYL LSRKRALWFS VSNDLKYDAE
RDLRDIGAKN ILVHSLNKFK YGKISSKHNG SVKKGVIFAT YSSLIGESQS GGKYKTRLKQ
LLHWCGDDFD GVIVFDECHK AKNLCPVGSS KPTKTGLAVL ELQNKLPKAR VVYASATGAS
EPRNMAYMNR LGIWGEGTPF REFSDFIQAV ERRGVGAMEI VAMDMKLRGM YIARQLSFTG
VTFKIEEVLL SQSYVKMYNK AVKLWVIARE RFQQAADLID AEQRMKKSMW GQFWSAHQRF
FKYLCIASKV KRVVQLAREE IKNGKCVVIG LQSTGEARTL EALEEGGGEL NDFVSTAKGV
LQSLIEKHFP APDRKKLYSL LGIDLTAPSN NSSPRDSPCK ENKIKKRKGE EITREAKKAR
KVGGLTGSSS DDSGSESDAS DNEESDYESS KNMSSGDDDD FNPFLDESNE DDENDPWLIR
KDHKKNKEKK KKKSIDPDSI QSALLASGLG SKRPSFSSTP VISPAPNSTP ANSNTNSNSS
LITSQDAVER AQQMKKDLLD KLEKLAEDLP PNTLDELIDE LGGPENVAEM TGRKGRVVSN
DDGSISYESR SELDVPVEIL NITEKQRFMD GDKNIAIISE AASSGISLQA DRRAKNQRRR
VHMTLELPWS ADRAIQQFGR THRSNQVTAP EYVFLISELA GEQRFASIVA KRLESLGALT
HGDRRATESR DLSRFNFDNK YGRNALEIVM KSIVNLDSPM VSPPPDYPGE FFKDVRQGLI
GVGLINVEDR SGILTLDKDY NNIGKFLNRI LGMEVHQQNA LFQYFADTLT AVVQNAKKNG
RYDMGILDLG SGDEKVRKSD VKKFLTPGYS TSGHVELYTI SVERGMSWEE ATKIWAELTG
PDDGFYLSLQ IRNNKKTAIL VKEVNPKKKL FLVYRPNTGK QLKLEIYADL KKKYKKVVSD
DALMHWLDQY NSSADTCTHA YWRGNCKKAS LGLVCEIGLR CRTYYVLCGS VLSVWTKVEG
VLASVSGTNV KMQIVRLRTE DGQRIVGLII PANCVSPLVN LLSTSDQSQQ LAVQQKQLWQ
QHHPQSITNL SNA
