ID U520_RAT Reviewed; 2139 AA.
AC F1LNJ2;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=U5 small nuclear ribonucleoprotein 200 kDa helicase;
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:O75643};
DE AltName: Full=BRR2 homolog;
DE AltName: Full=U5 snRNP-specific 200 kDa protein;
DE Short=U5-200KD;
GN Name=Snrnp200;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-709, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Catalyzes the ATP-dependent unwinding of U4/U6 RNA duplices,
CC an essential step in the assembly of a catalytically active
CC spliceosome. Plays a role in pre-mRNA splicing as core component of
CC precatalytic, catalytic and postcatalytic spliceosomal complexes. As a
CC component of the minor spliceosome, involved in the splicing of U12-
CC type introns in pre-mRNAs (By similarity). Involved in spliceosome
CC assembly, activation and disassembly. Mediates changes in the dynamic
CC network of RNA-RNA interactions in the spliceosome.
CC {ECO:0000250|UniProtKB:O75643}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000250|UniProtKB:O75643};
CC -!- SUBUNIT: Component of a core complex containing at least PRPF8,
CC SNRNP200, EFTUD2 and SNRNP40. Component of the U5 snRNP and U4/U6-U5
CC tri-snRNP complexes, building blocks of the spliceosome. Component of
CC the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and
CC at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40,
CC DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39. Component of
CC precatalytic, catalytic and postcatalytic spliceosomal complexes.
CC Component of the minor spliceosome, which splices U12-type introns (By
CC similarity). Interacts with C9orf78; the interaction is direct and
CC mutually exclusive with its interaction with WBP4. Interacts with WBP4;
CC the interaction is mutually exclusive with its interaction with
CC C9orf78. Interacts with PRPF8. Interacts with TSSC4; the interaction is
CC direct, excludes recruitment of C9ORF78 and WBP4 to SNRNP200 and
CC negatively regulates its RNA helicase activity (By similarity).
CC {ECO:0000250|UniProtKB:O75643}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75643}.
CC -!- DOMAIN: Contains two helicase domains. The N-terminal helicase domain
CC has catalytic activity by itself, contrary to C-terminal helicase
CC domain that may have a regulatory role and enhance the activity of the
CC first helicase domain. {ECO:0000250|UniProtKB:O75643}.
CC -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; F1LNJ2; -.
DR SMR; F1LNJ2; -.
DR IntAct; F1LNJ2; 1.
DR STRING; 10116.ENSRNOP00000048598; -.
DR CarbonylDB; F1LNJ2; -.
DR iPTMnet; F1LNJ2; -.
DR jPOST; F1LNJ2; -.
DR PaxDb; 10116-ENSRNOP00000048598; -.
DR Ensembl; ENSRNOT00000043895.5; ENSRNOP00000048598.4; ENSRNOG00000012157.8.
DR Ensembl; ENSRNOT00055008540; ENSRNOP00055006485; ENSRNOG00055005304.
DR Ensembl; ENSRNOT00060025090; ENSRNOP00060019985; ENSRNOG00060014656.
DR Ensembl; ENSRNOT00065021118; ENSRNOP00065016289; ENSRNOG00065012901.
DR AGR; RGD:1561120; -.
DR RGD; 1561120; Snrnp200.
DR eggNOG; KOG0951; Eukaryota.
DR InParanoid; F1LNJ2; -.
DR OMA; QTEIQYY; -.
DR TreeFam; TF300056; -.
DR Reactome; R-RNO-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-RNO-72165; mRNA Splicing - Minor Pathway.
DR PRO; PR:F1LNJ2; -.
DR Proteomes; UP000002494; Chromosome 3.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; ISO:RGD.
DR GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; ISS:UniProtKB.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; ISS:UniProtKB.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; ISO:RGD.
DR GO; GO:0005682; C:U5 snRNP; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0004386; F:helicase activity; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; ISS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0000388; P:spliceosome conformational change to release U4 (or U4atac) and U1 (or U11); ISO:RGD.
DR CDD; cd18019; DEXHc_Brr2_1; 1.
DR CDD; cd18021; DEXHc_Brr2_2; 1.
DR CDD; cd18795; SF2_C_Ski2; 2.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR Gene3D; 2.60.40.150; C2 domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR InterPro; IPR041094; Brr2_helicase_PWI.
DR InterPro; IPR048863; BRR2_plug.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004179; Sec63-dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR47961; DNA POLYMERASE THETA, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05260)-RELATED; 1.
DR PANTHER; PTHR47961:SF4; U5 SMALL NUCLEAR RIBONUCLEOPROTEIN HELICASE; 1.
DR Pfam; PF21188; BRR2_plug; 1.
DR Pfam; PF00270; DEAD; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF18149; Helicase_PWI; 1.
DR Pfam; PF02889; Sec63; 2.
DR PIRSF; PIRSF039073; BRR2; 1.
DR SMART; SM00487; DEXDc; 2.
DR SMART; SM00490; HELICc; 2.
DR SMART; SM00973; Sec63; 2.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
DR SUPFAM; SSF158702; Sec63 N-terminal domain-like; 2.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
DR PROSITE; PS51194; HELICASE_CTER; 2.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Coiled coil; Helicase; Hydrolase;
KW Isopeptide bond; mRNA processing; mRNA splicing; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein;
KW Spliceosome; Ubl conjugation.
FT CHAIN 1..2139
FT /note="U5 small nuclear ribonucleoprotein 200 kDa helicase"
FT /id="PRO_0000422050"
FT DOMAIN 490..673
FT /note="Helicase ATP-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 684..921
FT /note="Helicase C-terminal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 982..1289
FT /note="SEC63 1"
FT DOMAIN 1340..1515
FT /note="Helicase ATP-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1548..1756
FT /note="Helicase C-terminal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1815..2127
FT /note="SEC63 2"
FT REGION 39..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..2132
FT /note="Interaction with C9orf78 and WBP4"
FT /evidence="ECO:0000250|UniProtKB:O75643"
FT REGION 1285..2139
FT /note="Interaction with TSSC4"
FT /evidence="ECO:0000250|UniProtKB:O75643"
FT COILED 54..84
FT /evidence="ECO:0000255"
FT MOTIF 615..618
FT /note="DEAH box"
FT MOTIF 1457..1460
FT /note="DEAH box"
FT COMPBIAS 51..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 503..510
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 1353..1360
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75643"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75643"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 389
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75643"
FT MOD_RES 709
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 971
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O75643"
FT MOD_RES 1431
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75643"
FT MOD_RES 1768
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6P4T2"
FT MOD_RES 2005
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75643"
FT MOD_RES 2134
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75643"
FT MOD_RES 2136
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75643"
FT MOD_RES 2138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75643"
FT CROSSLNK 46
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75643"
FT CROSSLNK 944
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 971
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 1071
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 1199
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 2094
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 2139 AA; 244875 MW; C85E398D8032F98B CRC64;
MADVTARSLQ YEYKANSNLV LQADRSLIDR TRRDEPTGEV LSLVGKLEGT RMGDKAQRTK
PQMQEERRAK RRKRDEDRHD INKMKGYTLL SEGIDEMVGI IYKPKTKETR ETYEVLLSFI
QAALGDQPRD ILCGAADEVL AVLKNEKLRD KERRREIDLL LGQTDDTRYH VLVNLGKKIT
DYGGDKEIQN MDDNIDETYG VNVQFESDEE EGDEDVYGEV REEASDDDME GDEAVVRCTL
SANLVASGEL MSSKKKDLHP RDIDAFWLQR QLSRFYDDAI VSQKKADEVL EILKTASDDR
ECENQLVLLL GFNTFDFIKV LRQHRMMILY CTLLASAQSE AEKERIMGKM EADPELSKFL
YQLHETEKED LIREERSRRE RVRQSRMDTD LETMDLDQGG EALAPRQVLD LEDLVFTQGS
HFMANKRCQL PDGSFRRQRK GYEEVHVPAL KPKPFGSEEQ LLPVEKLPKY AQAGFEGFKT
LNRIQSKLYR AALETDENLL LCAPTGAGKT NVALMCMLRE IGKHINMDGT INVDDFKIIY
IAPMRSLVQE MVGSFGKRLA TYGITVAELT GDHQLCKEEI SATQIIVCTP EKWDIITRKG
GERTYTQLVR LIVLDEIHLL HDDRGPVLEA LVARAIRNIE MTQEDVRLIG LSATLPNYED
VATFLRVDPA KGLFYFDNSF RPVPLEQTYV GITEKKAIKR FQIMNEIVYE KIMEHAGKNQ
VLVFVHSRKE TGKTARAIRD MCLEKDTLGL FLREGSASTE VLRTEAEQCK NLELKDLLPY
GFAIHHAGMT RVDRTLVEDL FADKHIQVLV STATLAWGVN LPAHTVIIKG TQVYSPEKGR
WTELGALDIL QMLGRAGRPQ YDTKGEGILI TSHGELQYYL SLLNQQLPIE SQMVSKLPDM
LNAEIVLGNV QNAKDAVNWL GYAYLYIRML RSPTLYGISH DDLKGDPLLD QRRLDLVHTA
ALMLDKNNLV KYDKKTGNFQ VTELGRIASH YYITNDTVQT YNQLLKPTLS EIELFRVFSL
SSEFKNITVR EEEKLELQKL LERVPIPVKE SIEEPSAKIN VLLQAFISQL KLEGFALMAD
MVYVTQSAGR LMRAIFEIVL NRGWAQLTDK TLNLCKMIDK RMWQSMCPLR QFRKLPEEVV
KKIEKKNFPF ERLYDLNHNE IGELIRMPKM GKTIHKYVHL FPKLELSVHL QPITRSTLKV
ELTITPDFQW DEKARLVHGS SEAFWILVED VDSEVILHHE YFLLKAKYAQ DEHLITFFVP
VFEPLPPQYF IRVVSDRWLS CETQLPVSFR HLILPEKYPP PTELLDLQPL PVSALRNSAF
ESLYQDKFPF FNPIQTQVFN TVYNSDDNVF VGAPTGSGKT ICAEFAILRM LLQNSEGRCV
YITPMEALAE QVYMDWYEKF QDRLNKKVVL LTGETSTDLK LLGKGNIIIS TPEKWDILSR
RWKQRKNVQN INLFVVDEVH LIGGENGPVL EVICSRMRYI SSQIERPIRI VALSSSLSNA
KDVAHWLGCS ATSTFNFHPN VRPVPLELHI QGFNISHTQT RLLSMAKPVY HAITKHSPKK
PVIVFVPSRK QTRLTAIDIL TTCAADIQRQ RFLHCTEKDL IPYLEKLSDS TLKETLLNGV
GYLHEGLSPM ERRLVEQLFS SGAIQVVVAS RSLCWGMNVA AHLVIIMDTQ YYNGKIHAYV
DYPIYDVLQM VGHANRPLQD DEGRCVIMCQ GSKKDFFKKF LYEPLPVESH LDHCMHDHFN
AEIVTKTIEN KQDAVDYLTW TFLYRRMTQN PNYYNLQGIS HRHLSDHLSE LVEQTLSDLE
QSKCISIEDE MDVAPLNLGM IAAYYYINYT TIELFSMSLN AKTKVRGLIE IISNAAEYEN
IPIRHHEDNL LRQLAQKVPH KLNNPKFNDP HVKTNLLLQA HLSRMQLSAE LQSDTEEILS
KAIRLIQACV DVLSSNGWLS PALAAMELAQ MVTQAMWSKD SYLKQLPHFT SEHIKRCTDK
GVESVFDIME MEDEERNALL QLTDSQIADV ARFCNRYPNI ELSYEVVDKD SIRSGGPVVV
LVQLEREEEV TGPVIAPLFP QKREEGWWVV IGDAKSNSLI SIKRLTLQQK AKVKLDFVAP
ATGGHNYTLY FMSDAYMGCD QEYKFSVDVK EAETDSDSD
//
