ID HECW1_HUMAN Reviewed; 1606 AA.
AC Q76N89; A7E2X0; A8MYS3; B4DH42; O15036; Q9HCC7;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 3.
DT 27-MAR-2024, entry version 162.
DE RecName: Full=E3 ubiquitin-protein ligase HECW1;
DE EC=2.3.2.26;
DE AltName: Full=HECT, C2 and WW domain-containing protein 1;
DE AltName: Full=HECT-type E3 ubiquitin transferase HECW1;
DE AltName: Full=NEDD4-like E3 ubiquitin-protein ligase 1;
DE Short=hNEDL1;
GN Name=HECW1; Synonyms=KIAA0322, NEDL1;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-1606 (ISOFORM 1), FUNCTION, INTERACTION
RP WITH DVL1; SSR3 AND SOD1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=14684739; DOI=10.1074/jbc.m312389200;
RA Miyazaki K., Fujita T., Ozaki T., Kato C., Kurose Y., Sakamoto M., Kato S.,
RA Goto T., Itoyama Y., Aoki M., Nakagawara A.;
RT "NEDL1, a novel ubiquitin-protein isopeptide ligase for dishevelled-1,
RT targets mutant superoxide dismutase-1.";
RL J. Biol. Chem. 279:11327-11335(2004).
RN [7]
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).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and
CC subsequent degradation of DVL1. Also targets the mutant SOD1 protein
CC involved in familial amyotrophic lateral sclerosis (FALS). Forms
CC cytotoxic aggregates with DVL1, SSR3 and mutant SOD1 that lead to motor
CC neuron death in FALS. {ECO:0000269|PubMed:14684739}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.26;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with DVL1 and SSR3. Also interacts with mutant SOD1.
CC {ECO:0000269|PubMed:14684739}.
CC -!- INTERACTION:
CC Q76N89; Q5SQQ9-2: VAX1; NbExp=3; IntAct=EBI-949582, EBI-12227803;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14684739}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q76N89-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q76N89-2; Sequence=VSP_054642;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in neurons of adult and
CC fetal brain. Weakly expressed in the kidney.
CC {ECO:0000269|PubMed:14684739}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA20780.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB002320; BAA20780.2; ALT_INIT; mRNA.
DR EMBL; AK294918; BAG58003.1; -; mRNA.
DR EMBL; AC004455; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC004692; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005537; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC006365; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011738; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC151227; AAI51228.1; -; mRNA.
DR EMBL; AB048365; BAB13352.1; -; mRNA.
DR CCDS; CCDS5469.2; -. [Q76N89-1]
DR CCDS; CCDS69286.1; -. [Q76N89-2]
DR RefSeq; NP_001273988.1; NM_001287059.1. [Q76N89-2]
DR RefSeq; NP_055867.3; NM_015052.4. [Q76N89-1]
DR RefSeq; XP_016867375.1; XM_017011886.1.
DR RefSeq; XP_016867378.1; XM_017011889.1.
DR PDB; 3L4H; X-ray; 1.80 A; A=948-1056.
DR PDBsum; 3L4H; -.
DR AlphaFoldDB; Q76N89; -.
DR SMR; Q76N89; -.
DR BioGRID; 116705; 40.
DR IntAct; Q76N89; 12.
DR MINT; Q76N89; -.
DR STRING; 9606.ENSP00000379228; -.
DR GlyCosmos; Q76N89; 1 site, 1 glycan.
DR GlyGen; Q76N89; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q76N89; -.
DR PhosphoSitePlus; Q76N89; -.
DR BioMuta; HECW1; -.
DR DMDM; 223590222; -.
DR EPD; Q76N89; -.
DR jPOST; Q76N89; -.
DR MassIVE; Q76N89; -.
DR MaxQB; Q76N89; -.
DR PaxDb; 9606-ENSP00000379228; -.
DR PeptideAtlas; Q76N89; -.
DR ProteomicsDB; 4192; -.
DR ProteomicsDB; 68692; -. [Q76N89-1]
DR Antibodypedia; 1996; 71 antibodies from 16 providers.
DR DNASU; 23072; -.
DR Ensembl; ENST00000395891.7; ENSP00000379228.1; ENSG00000002746.15. [Q76N89-1]
DR Ensembl; ENST00000453890.5; ENSP00000407774.1; ENSG00000002746.15. [Q76N89-2]
DR GeneID; 23072; -.
DR KEGG; hsa:23072; -.
DR MANE-Select; ENST00000395891.7; ENSP00000379228.1; NM_015052.5; NP_055867.3.
DR UCSC; uc003tid.2; human. [Q76N89-1]
DR AGR; HGNC:22195; -.
DR CTD; 23072; -.
DR DisGeNET; 23072; -.
DR GeneCards; HECW1; -.
DR HGNC; HGNC:22195; HECW1.
DR HPA; ENSG00000002746; Tissue enhanced (brain, kidney).
DR MIM; 610384; gene.
DR neXtProt; NX_Q76N89; -.
DR OpenTargets; ENSG00000002746; -.
DR PharmGKB; PA134964191; -.
DR VEuPathDB; HostDB:ENSG00000002746; -.
DR eggNOG; KOG0940; Eukaryota.
DR GeneTree; ENSGT00940000158294; -.
DR HOGENOM; CLU_002173_14_0_1; -.
DR InParanoid; Q76N89; -.
DR OMA; SGSQNCE; -.
DR OrthoDB; 5480520at2759; -.
DR PhylomeDB; Q76N89; -.
DR TreeFam; TF313938; -.
DR BRENDA; 2.3.2.26; 2681.
DR PathwayCommons; Q76N89; -.
DR Reactome; R-HSA-4641258; Degradation of DVL.
DR SignaLink; Q76N89; -.
DR SIGNOR; Q76N89; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 23072; 11 hits in 1185 CRISPR screens.
DR ChiTaRS; HECW1; human.
DR EvolutionaryTrace; Q76N89; -.
DR GenomeRNAi; 23072; -.
DR Pharos; Q76N89; Tbio.
DR PRO; PR:Q76N89; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q76N89; Protein.
DR Bgee; ENSG00000002746; Expressed in Brodmann (1909) area 23 and 126 other cell types or tissues.
DR ExpressionAtlas; Q76N89; baseline and differential.
DR Genevisible; Q76N89; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:Reactome.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; IBA:GO_Central.
DR CDD; cd08691; C2_NEDL1-like; 1.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd00201; WW; 2.
DR Gene3D; 2.20.70.10; -; 2.
DR Gene3D; 2.60.40.2840; -; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037795; C2_HECW.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR040524; HECW1_helix.
DR InterPro; IPR032348; HECW_N.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR11254:SF79; E3 UBIQUITIN-PROTEIN LIGASE HECW1; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF18436; HECW1_helix; 1.
DR Pfam; PF16562; HECW_N; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF51045; WW domain; 2.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 2.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Phosphoprotein;
KW Reference proteome; Repeat; Transferase; Ubl conjugation pathway.
FT CHAIN 1..1606
FT /note="E3 ubiquitin-protein ligase HECW1"
FT /id="PRO_0000277665"
FT DOMAIN 182..318
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 829..862
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 1018..1051
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 1271..1606
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT REGION 349..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 870..901
FT /evidence="ECO:0000255"
FT COMPBIAS 357..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..503
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 920..938
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1574
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT MOD_RES 874
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K4P8"
FT MOD_RES 937
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K4P8"
FT MOD_RES 939
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K4P8"
FT VAR_SEQ 800..834
FT /note="GECPILHNSQPVSQLPSLRPEHHHYPTIDEPLPPN -> D (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054642"
FT CONFLICT 404
FT /note="G -> R (in Ref. 1; BAA20780, 4; AAI51228 and 5;
FT BAB13352)"
FT /evidence="ECO:0000305"
FT HELIX 953..958
FT /evidence="ECO:0007829|PDB:3L4H"
FT HELIX 963..968
FT /evidence="ECO:0007829|PDB:3L4H"
FT HELIX 971..979
FT /evidence="ECO:0007829|PDB:3L4H"
FT HELIX 982..992
FT /evidence="ECO:0007829|PDB:3L4H"
FT HELIX 995..1000
FT /evidence="ECO:0007829|PDB:3L4H"
FT HELIX 1004..1011
FT /evidence="ECO:0007829|PDB:3L4H"
FT STRAND 1024..1028
FT /evidence="ECO:0007829|PDB:3L4H"
FT STRAND 1034..1038
FT /evidence="ECO:0007829|PDB:3L4H"
FT TURN 1039..1042
FT /evidence="ECO:0007829|PDB:3L4H"
FT STRAND 1043..1047
FT /evidence="ECO:0007829|PDB:3L4H"
SQ SEQUENCE 1606 AA; 179554 MW; 22AE698F16276E98 CRC64;
MLLHLCSVKN LYQNRFLGLA AMASPSRNSQ SRRRCKEPLR YSYNPDQFHN MDLRGGPHDG
VTIPRSTSDT DLVTSDSRST LMVSSSYYSI GHSQDLVIHW DIKEEVDAGD WIGMYLIDEV
LSENFLDYKN RGVNGSHRGQ IIWKIDASSY FVEPETKICF KYYHGVSGAL RATTPSVTVK
NSAAPIFKSI GADETVQGQG SRRLISFSLS DFQAMGLKKG MFFNPDPYLK ISIQPGKHSI
FPALPHHGQE RRSKIIGNTV NPIWQAEQFS FVSLPTDVLE IEVKDKFAKS RPIIKRFLGK
LSMPVQRLLE RHAIGDRVVS YTLGRRLPTD HVSGQLQFRF EITSSIHPDD EEISLSTEPE
SAQIQDSPMN NLMESGSGEP RSEAPESSES WKPEQLGEGS VPDGPGNQSI ELSRPAEEAA
VITEAGDQGM VSVGPEGAGE LLAQVQKDIQ PAPSAEELAE QLDLGEEASA LLLEDGEAPA
STKEEPLEEE ATTQSRAGRE EEEKEQEEEG DVSTLEQGEG RLQLRASVKR KSRPCSLPVS
ELETVIASAC GDPETPRTHY IRIHTLLHSM PSAQGGSAAE EEDGAEEEST LKDSSEKDGL
SEVDTVAADP SALEEDREEP EGATPGTAHP GHSGGHFPSL ANGAAQDGDT HPSTGSESDS
SPRQGGDHSC EGCDASCCSP SCYSSSCYST SCYSSSCYSA SCYSPSCYNG NRFASHTRFS
SVDSAKISES TVFSSQDDEE EENSAFESVP DSMQSPELDP ESTNGAGPWQ DELAAPSGHV
ERSPEGLESP VAGPSNRREG ECPILHNSQP VSQLPSLRPE HHHYPTIDEP LPPNWEARID
SHGRVFYVDH VNRTTTWQRP TAAATPDGMR RSGSIQQMEQ LNRRYQNIQR TIATERSEED
SGSQSCEQAP AGGGGGGGSD SEAESSQSSL DLRREGSLSP VNSQKITLLL QSPAVKFITN
PEFFTVLHAN YSAYRVFTSS TCLKHMILKV RRDARNFERY QHNRDLVNFI NMFADTRLEL
PRGWEIKTDQ QGKSFFVDHN SRATTFIDPR IPLQNGRLPN HLTHRQHLQR LRSYSAGEAS
EVSRNRGASL LARPGHSLVA AIRSQHQHES LPLAYNDKIV AFLRQPNIFE MLQERQPSLA
RNHTLREKIH YIRTEGNHGL EKLSCDADLV ILLSLFEEEI MSYVPLQAAF HPGYSFSPRC
SPCSSPQNSP GLQRASARAP SPYRRDFEAK LRNFYRKLEA KGFGQGPGKI KLIIRRDHLL
EGTFNQVMAY SRKELQRNKL YVTFVGEEGL DYSGPSREFF FLLSQELFNP YYGLFEYSAN
DTYTVQISPM SAFVENHLEW FRFSGRILGL ALIHQYLLDA FFTRPFYKAL LRLPCDLSDL
EYLDEEFHQS LQWMKDNNIT DILDLTFTVN EEVFGQVTER ELKSGGANTQ VTEKNKKEYI
ERMVKWRVER GVVQQTEALV RGFYEVVDSR LVSVFDAREL ELVIAGTAEI DLNDWRNNTE
YRGGYHDGHL VIRWFWAAVE RFNNEQRLRL LQFVTGTSSV PYEGFAALRG SNGLRRFCIE
KWGKITSLPR AHTCFNRLDL PPYPSYSMLY EKLLTAVEET STFGLE
//
