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   27-MAR-2024, entry version 127.
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; 71.
DR   IntAct; A3KN83; 9.
DR   MINT; A3KN83; -.
DR   STRING; 9606.ENSP00000473665; -.
DR   GlyConnect; 2874; 1 O-GlcNAc glycan (1 site).
DR   GlyCosmos; A3KN83; 10 sites, 2 glycans.
DR   GlyGen; A3KN83; 13 sites, 2 O-linked glycans (13 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; 9606-ENSP00000387361; -.
DR   PeptideAtlas; A3KN83; -.
DR   ProteomicsDB; 582; -. [A3KN83-1]
DR   ProteomicsDB; 583; -. [A3KN83-2]
DR   ProteomicsDB; 584; -. [A3KN83-3]
DR   ProteomicsDB; 585; -. [A3KN83-4]
DR   Pumba; A3KN83; -.
DR   Antibodypedia; 52514; 54 antibodies from 15 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   AGR; HGNC:22973; -.
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; CEIGLRT; -.
DR   OrthoDB; 3541637at2759; -.
DR   PhylomeDB; A3KN83; -.
DR   TreeFam; TF313526; -.
DR   PathwayCommons; A3KN83; -.
DR   SignaLink; A3KN83; -.
DR   BioGRID-ORCS; 55206; 715 hits in 1168 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 male germ line stem cell (sensu Vertebrata) in testis and 197 other cell types or tissues.
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:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR   GO; GO:0048583; P:regulation of response to stimulus; IEA:UniProt.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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:SF8; PROTEIN STRAWBERRY NOTCH HOMOLOG 1; 1.
DR   PANTHER; PTHR12706; STRAWBERRY NOTCH-RELATED; 1.
DR   Pfam; PF13872; AAA_34; 1.
DR   Pfam; PF13871; Helicase_C_4; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   Genevisible; A3KN83; HS.
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
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