ID   ERC6L_MOUSE             Reviewed;        1240 AA.
AC   Q8BHK9; Q8BGN1; Q8BRC9; Q8CE49;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 156.
DE   RecName: Full=DNA excision repair protein ERCC-6-like;
DE            EC=3.6.4.12 {ECO:0000250|UniProtKB:Q2NKX8};
DE   AltName: Full=ATP-dependent helicase ERCC6-like;
GN   Name=Ercc6l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ; TISSUE=Heart;
RA   Chen X.-G., Li Y., Zang M.-X., Pei X.-R., Xu Y.-J., Fang L.-F.;
RT   "cDNA cloning and expression analysis of mouse gene encoding the protein
RT   Ercc6l which is a novel member of SNF2 family.";
RL   Sheng Wu Hua Xue Yu Sheng Wu Wu Li Jin Zhan 31:443-448(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Heart, and Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
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   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=15917148; DOI=10.1016/j.toxlet.2005.02.013;
RA   Xu Y.-J., Chen X.-G., Li Y.;
RT   "Ercc6l, a gene of SNF2 family, may play a role in the teratogenic action
RT   of alcohol.";
RL   Toxicol. Lett. 157:233-239(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1021, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-998; SER-1001; SER-1021 AND
RP   SER-1112, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Lung, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: DNA helicase that acts as a tension sensor that associates
CC       with catenated DNA which is stretched under tension until it is
CC       resolved during anaphase. Functions as ATP-dependent DNA translocase.
CC       Can promote Holliday junction branch migration (in vitro).
CC       {ECO:0000250|UniProtKB:Q2NKX8}.
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=3.6.4.12;
CC         Evidence={ECO:0000250|UniProtKB:Q2NKX8};
CC   -!- SUBUNIT: Interacts with PLK1, which phosphorylates it. Both proteins
CC       are mutually dependent on each other for correct subcellular
CC       localization. Interacts (via N-terminal TPR repeat) with BEND3 (via BEN
CC       domains 1 and 3); the interaction is direct.
CC       {ECO:0000250|UniProtKB:Q2NKX8}.
CC   -!- SUBCELLULAR LOCATION: Chromosome, centromere
CC       {ECO:0000250|UniProtKB:Q2NKX8}. Chromosome, centromere, kinetochore
CC       {ECO:0000250|UniProtKB:Q2NKX8}. Chromosome
CC       {ECO:0000250|UniProtKB:Q2NKX8}. Note=Localizes to kinetochores, inner
CC       centromeres and thin threads connecting separating chromosomes even
CC       during anaphase. In prometaphase cells, it mostly concentrates in
CC       between kinetochores. In metaphase, it localizes to numerous thin
CC       threads that stretch between sister kinetochores of the aligned
CC       chromosomes and are composed of catenated centromeric DNA. Evolution
CC       from inner centromeres to thin threads takes place in response to
CC       tension. Resolution of thin threads requires topoisomerase 2-alpha
CC       (TOP2A) after anaphase onset. {ECO:0000250|UniProtKB:Q2NKX8}.
CC   -!- TISSUE SPECIFICITY: Expressed mainly in the neural tube and heart of
CC       10.5 dpc embryo. Significantly down-regulated after alcohol exposure in
CC       embryonic brain and heart, but not in embryonic kidney, liver, or lung.
CC       {ECO:0000269|PubMed:15917148}.
CC   -!- PTM: Phosphorylation by PLK1 prevents the association with chromosome
CC       arms and restricts its localization to the kinetochore-centromere
CC       region. {ECO:0000250|UniProtKB:Q2NKX8}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {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   EMBL; AY172688; AAN87172.1; -; mRNA.
DR   EMBL; AK029015; BAC26244.1; -; mRNA.
DR   EMBL; AK045113; BAC32227.2; -; mRNA.
DR   EMBL; AK084617; BAC39230.1; -; mRNA.
DR   EMBL; AK084618; BAC39231.1; -; mRNA.
DR   EMBL; AL807784; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC037660; AAH37660.1; -; mRNA.
DR   CCDS; CCDS30321.1; -.
DR   RefSeq; NP_666347.2; NM_146235.3.
DR   AlphaFoldDB; Q8BHK9; -.
DR   SMR; Q8BHK9; -.
DR   BioGRID; 231820; 35.
DR   IntAct; Q8BHK9; 33.
DR   STRING; 10090.ENSMUSP00000050592; -.
DR   GlyGen; Q8BHK9; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8BHK9; -.
DR   PhosphoSitePlus; Q8BHK9; -.
DR   EPD; Q8BHK9; -.
DR   jPOST; Q8BHK9; -.
DR   MaxQB; Q8BHK9; -.
DR   PaxDb; 10090-ENSMUSP00000050592; -.
DR   PeptideAtlas; Q8BHK9; -.
DR   ProteomicsDB; 275768; -.
DR   Pumba; Q8BHK9; -.
DR   Antibodypedia; 27876; 240 antibodies from 28 providers.
DR   DNASU; 236930; -.
DR   Ensembl; ENSMUST00000056904.3; ENSMUSP00000050592.3; ENSMUSG00000051220.3.
DR   GeneID; 236930; -.
DR   KEGG; mmu:236930; -.
DR   UCSC; uc009tyk.2; mouse.
DR   AGR; MGI:2654144; -.
DR   CTD; 54821; -.
DR   MGI; MGI:2654144; Ercc6l.
DR   VEuPathDB; HostDB:ENSMUSG00000051220; -.
DR   eggNOG; KOG0387; Eukaryota.
DR   GeneTree; ENSGT00940000156837; -.
DR   HOGENOM; CLU_004666_0_0_1; -.
DR   InParanoid; Q8BHK9; -.
DR   OMA; FTIEDFQ; -.
DR   OrthoDB; 5485325at2759; -.
DR   PhylomeDB; Q8BHK9; -.
DR   TreeFam; TF332843; -.
DR   Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR   Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR   Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR   Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-MMU-68877; Mitotic Prometaphase.
DR   Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR   BioGRID-ORCS; 236930; 22 hits in 117 CRISPR screens.
DR   ChiTaRS; Ercc6l; mouse.
DR   PRO; PR:Q8BHK9; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; Q8BHK9; Protein.
DR   Bgee; ENSMUSG00000051220; Expressed in primary oocyte and 140 other cell types or tissues.
DR   GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0015616; F:DNA translocase activity; ISS:UniProtKB.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   CDD; cd18001; DEXHc_ERCC6L; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45629:SF7; DNA EXCISION REPAIR PROTEIN ERCC-6-RELATED; 1.
DR   PANTHER; PTHR45629; SNF2/RAD54 FAMILY MEMBER; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   Genevisible; Q8BHK9; MM.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell cycle; Cell division; Centromere; Chromosome;
KW   DNA-binding; Helicase; Hydrolase; Kinetochore; Mitosis; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Repeat; TPR repeat.
FT   CHAIN           1..1240
FT                   /note="DNA excision repair protein ERCC-6-like"
FT                   /id="PRO_0000328832"
FT   REPEAT          21..54
FT                   /note="TPR 1"
FT   DOMAIN          110..278
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          467..631
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REPEAT          1191..1224
FT                   /note="TPR 2"
FT   REGION          736..760
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          778..813
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          845..879
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          974..1085
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1104..1185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           229..232
FT                   /note="DEAH box"
FT   COMPBIAS        796..813
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        978..998
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        999..1022
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1035..1085
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1104..1130
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1137..1160
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1161..1177
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         123..130
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOD_RES         14
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q2NKX8"
FT   MOD_RES         755
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q2NKX8"
FT   MOD_RES         773
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q2NKX8"
FT   MOD_RES         821
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q2NKX8"
FT   MOD_RES         966
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q2NKX8"
FT   MOD_RES         998
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1001
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1021
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         1057
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q2NKX8"
FT   MOD_RES         1092
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q2NKX8"
FT   MOD_RES         1112
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1172
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q2NKX8"
FT   CONFLICT        1210
FT                   /note="A -> S (in Ref. 2; BAC26244)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1240 AA;  138854 MW;  0B996A4286F51C27 CRC64;
     MEASQGLAEV ETLSPQLAES YLRYVQEAKE AAKNGDLEES LKLFNLAKDI FPTKKVMSRI
     QKLQEALEQL AEEEDDDEFI DVCSSGLLLY RELYEKLFEH QKEGIAFLYS LYKDGRKGGI
     LADDMGLGKT VQIIAFLSGM FDASLVNHVL LIMPTNLINT WVNEFAKWTP GMRVKTFHGS
     SKSERTRSLT RIQQRNGVVI TTYQMLLNNW QQLASFNGQA FVWDYVILDE AHKIKSASTK
     SAVCARAIPA SNRLLLTGTP VQNNLQELWS LFDFACQGSL LGTLKTFKME YEHPIIRARE
     KDATPGEKAL GLKISENLME IIKPYFLRRT KEEVQTKKAD NPEARLGEKN PAGEAICDMF
     SLARKNDLIV WIRLLPLQEE IYRKFVSLDH IKELLMETRS PLAELGVLKK LCDHPRLLSA
     RACRLLNLGT ATFSAQDENE QEDVSNMNSI DHLPDKTLIQ ESGKMIFLMS LLERLQDEGH
     QTLVFSQSIK ILNIIERLLK NKHFKTLRID GTVTHLWERE KRIQLFQQNK EYSVFLLTTQ
     VGGVGLTLTA ATRVVIFDPS WNPATDAQAV DRVYRIGQKE NVVVYRLITC GTVEEKIYRR
     QVFKDSLIRQ TTGEKKNPFR YFTKQELKEL FTVGDLQKSA TQMQLQCLHA AQRRSDEKLD
     EHIAYLHLLG IAGISDHDLM FTRDLSVKEE LDMLEDSQYI HQRVQKAQFL VESESQNTVQ
     RQTTGIEETW LKAQEFPSQQ KKKGTEFNKP QPQPSRLLTK PTQVEAISSQ MASITICDQS
     AESEPQEHSE VHDVTSLQGS HHFNSTSDAG TIASLPQGAE SIGEVSTDSL LSPAKGFAAE
     NDAMQKKGLQ ASPGQEAPSE NLGSFHYLPR ESSKASLGPN LDLQDSVVLY HRSPTANENQ
     NLESDVPMIE ISDDLSEPPS ALQGAQAIEA QLELKEDDPL KSPPQYACDF NLFLEDSADT
     RQNLSSKFLE HVEKEKSLQS PAANSRAKSA LTLSLDSSPK SDEESEVISV KTKSKTRRIL
     SDDEDEDEED AFKGSHTNSI NISPFPFSSV KQFDASTPQS GSNPSRRFFS PKTPGEVNTS
     LHSRRSLASR RSLINVVLDD VEDMEERLDN SSEEESEPGL SEENNEEEAL ACTEEQPSGA
     TLASGNKSSN LTMSEPTSPA PQSSPCAPEP SSSDPMPDPP QDLAVEAGND YESLVARGKE
     LKECGKIQEA LNCLVKALDI KSADPEVMLM TLSLYKQLNI
//