TRIPC_RAT
ID TRIPC_RAT Reviewed; 2025 AA.
AC F1LP64; F1LP79; Q497C1; Q5I0I0;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=E3 ubiquitin-protein ligase TRIP12;
DE EC=2.3.2.26 {ECO:0000250|UniProtKB:Q14669};
DE AltName: Full=HECT-type E3 ubiquitin transferase TRIP12;
DE AltName: Full=Thyroid receptor-interacting protein 12;
DE Short=TR-interacting protein 12;
DE Short=TRIP-12;
GN Name=Trip12;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Liver, and Prostate;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; SER-312; SER-1024;
RP SER-1049; SER-1350; SER-1355; SER-1409 AND THR-1410, 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: E3 ubiquitin-protein ligase involved in ubiquitin fusion
CC degradation (UFD) pathway and regulation of DNA repair. Part of the
CC ubiquitin fusion degradation (UFD) pathway, a process that mediates
CC ubiquitination of protein at their N-terminus, regardless of the
CC presence of lysine residues in target proteins. Acts as a key regulator
CC of DNA damage response by acting as a suppressor of RNF168, an E3
CC ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked
CC histone H2A and H2AX at DNA damage sites, thereby acting as a guard
CC against excessive spreading of ubiquitinated chromatin at damaged
CC chromosomes. In normal cells, mediates ubiquitination and degradation
CC of isoform p19ARF/ARF of CDKN2A, a lysine-less tumor suppressor
CC required for p53/TP53 activation under oncogenic stress. In cancer
CC cells, however, isoform p19ARF/ARF and TRIP12 are located in different
CC cell compartments, preventing isoform p19ARF/ARF ubiquitination and
CC degradation. Does not mediate ubiquitination of isoform p16-INK4a of
CC CDKN2A. Also catalyzes ubiquitination of NAE1 and SMARCE1, leading to
CC their degradation. Ubiquitination and degradation of target proteins is
CC regulated by interaction with proteins such as MYC, TRADD or SMARCC1,
CC which disrupt the interaction between TRIP12 and target proteins.
CC Mediates ubiquitination of ASXL1: following binding to N(6)-
CC methyladenosine methylated DNA, ASXL1 is ubiquitinated by TRIP12,
CC leading to its degradation and subsequent inactivation of the PR-DUB
CC complex. {ECO:0000250|UniProtKB:Q14669}.
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; Evidence={ECO:0000250|UniProtKB:Q14669};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q14669}.
CC -!- SUBUNIT: Interacts with MYC; leading to disrupt interaction with
CC isoform p19ARF/ARF of CDKN2A. Interacts with TRADD; leading to disrupt
CC interaction with isoform p19ARF/ARF of CDKN2A. Interacts with SMARCC1;
CC leading to disrupt interaction with SMARCE1.
CC {ECO:0000250|UniProtKB:Q14669}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q14669}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F1LP64-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F1LP64-2; Sequence=VSP_044332;
CC -!- SIMILARITY: Belongs to the UPL family. K-HECT subfamily. {ECO:0000305}.
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DR EMBL; BC088304; AAH88304.1; -; mRNA.
DR EMBL; BC100624; AAI00625.1; -; mRNA.
DR RefSeq; NP_001026829.2; NM_001031659.2. [F1LP64-1]
DR AlphaFoldDB; F1LP64; -.
DR SMR; F1LP64; -.
DR BioGRID; 261382; 2.
DR IntAct; F1LP64; 8.
DR STRING; 10116.ENSRNOP00000022822; -.
DR iPTMnet; F1LP64; -.
DR PhosphoSitePlus; F1LP64; -.
DR jPOST; F1LP64; -.
DR PaxDb; F1LP64; -.
DR PRIDE; F1LP64; -.
DR GeneID; 316575; -.
DR KEGG; rno:316575; -.
DR UCSC; RGD:1306607; rat.
DR CTD; 9320; -.
DR RGD; 1306607; Trip12.
DR VEuPathDB; HostDB:ENSRNOG00000016963; -.
DR eggNOG; KOG0168; Eukaryota.
DR eggNOG; KOG0170; Eukaryota.
DR InParanoid; F1LP64; -.
DR OrthoDB; 34110at2759; -.
DR TreeFam; TF323674; -.
DR Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:F1LP64; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000016963; Expressed in testis and 20 other tissues.
DR ExpressionAtlas; F1LP64; baseline and differential.
DR GO; GO:0016607; C:nuclear speck; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; ISO:RGD.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:2000780; P:negative regulation of double-strand break repair; ISS:UniProtKB.
DR GO; GO:1901315; P:negative regulation of histone H2A K63-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR GO; GO:2000779; P:regulation of double-strand break repair; IBA:GO_Central.
DR GO; GO:0045995; P:regulation of embryonic development; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR CDD; cd00078; HECTc; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 3.30.720.50; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR045322; HECTD1/TRIP12-like.
DR InterPro; IPR004170; WWE-dom.
DR InterPro; IPR018123; WWE-dom_subgr.
DR InterPro; IPR037197; WWE_dom_sf.
DR PANTHER; PTHR45670; PTHR45670; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF02825; WWE; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00678; WWE; 1.
DR SUPFAM; SSF117839; SSF117839; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF56204; SSF56204; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS50918; WWE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; DNA damage; DNA repair; Nucleus;
KW Phosphoprotein; Reference proteome; Transferase; Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q14669"
FT CHAIN 2..2025
FT /note="E3 ubiquitin-protein ligase TRIP12"
FT /id="PRO_0000419690"
FT DOMAIN 755..869
FT /note="WWE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00248"
FT DOMAIN 1918..2025
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT REGION 1..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 970..1077
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1440..1466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1529..1603
FT /note="K-box"
FT /evidence="ECO:0000250"
FT REGION 1601..1620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..359
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..1020
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1060
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1061..1077
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1992
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q14669"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14669"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:G5E870"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14669"
FT MOD_RES 181
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:G5E870"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14669"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 975
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14669"
FT MOD_RES 1024
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1030
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14669"
FT MOD_RES 1049
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1063
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14669"
FT MOD_RES 1350
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1355
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1362
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:G5E870"
FT MOD_RES 1409
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1410
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1458
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:G5E870"
FT MOD_RES 1460
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:G5E870"
FT VAR_SEQ 1374..1422
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044332"
SQ SEQUENCE 2025 AA; 223928 MW; 65FDA276207D2D5D CRC64;
MSNRPNNNPG GSLRRSQRNT AGAQPQDDSI GGRSCSSSSA VIVPQPEDPD RANTSERQKT
GQVPKKDNSR GVKRSASPDY NRTNSPSSAK KPRAFQHIES LSETNKPPSK SKKRHLDQEQ
QLKSAQLPST SKAHTRKSVA AGSSRSQKRK RTESSCVKSG SGSESTGAEE RSAKPTKLAS
KSATSAKAGC STITDSSSAA STSSSSSAVA SASSTVPAGA RVKQGKDQNK ARRSRSASSP
SPRRSSREKE QSKTGGSSKF DWAARFSPKV SLPKTKLSLP GSSKSETSKP GPSGLQAKLA
SLRKSTKKRS ESPPAELPSL RRSTRQKTTG SCASTSRRGS GLGKRGAAEA RRQEKMADPE
GNQETVNSSA ARTDEAPQGA AASSSVAGAV GMTTSGESES DDSEMGRLQA LLEARGLPPH
LFGPLGPRMS QLFHRTIGSG ASSKAQQLLQ GLQASDESQQ LQAVIEMCQL LVMGNEETLG
GFPVKSVVPA LITLLQMEHN FDIMNHACRA LTYMMEALPR SSAVVVDAIP VFLEKLQVIQ
CIDVAEQALT ALEMLSRRHS KAILQAGGLA DCLLYLEFFS INAQRNALAI AANCCQSITP
DEFHFVADSL PLLTQRLTHQ DKKSVESTCL CFARLVDNFQ HEENLLQQVA SKDLLTNVQQ
LLVVTPPILS SGMFIMVVRM FSLMCSNCPT LAVQLMKQNI AETLHFLLCG ASNGSCQEQI
DLVPRSPQEL YELTSLICEL MPCLPKEGIF AVDTMLKKGN AQNTDGAIWQ WRDDRGLWHP
YNRIDSRIIE AAHQVGEDEI SLSTLGRVYT IDFNSMQQIN EDTGTARAIQ RKPNPLANTN
TSGYSDLKKD DARAQLMKED PELAKSFIKT LFGVLYEVYS SSAGPAVRHK CLRAILRIIY
FADAELLKDV LKNHAVSSHI ASMLSSQDLK IVVGALQMAE ILMQKLPDIF SVYFRREGVM
HQVKHLAESE SLLTSPPKAC TNGSGSLGST TPASSGTATA ATNASADLGS PSLQHSRDDS
LDLSPQGRLS DVLKRKRLPK RGPRRPKYSP PRDDDKVDNQ AKSPTTTQSP KSSFLASLNP
KTWGRLSAQS NSNNIEPART AGVSGLARAA SKDTISNNRE KIKGWIKEQA HKFVERYFSS
ENMDGSNPAL NVLQRLCAAT EQLNLQVDGG AECLVEIRSI VSESDVSSFE IQHSGFVKQL
LLYLTSKSEK DAVSREIRLK RFLHVFFSSP LPGEEPVGRV EPVGHAPLLA LVHKMNNCLS
QMEQFPVKVH DFPSGNGSGG SFSLNRGSQA LKFFNTHQLK CQLQRHPDCA NVKQWKGGPV
KIDPLALVQA IERYLVVRGY GRVREDDEDS DDDGSDEEID ESLAAQFLNS GNVRHRLQFY
IGEHLLPYNM TVYQAVRQFS VQAEDEREST DDESNPLGRA GIWTKTHTIW YKPVREDEES
SKDCVGGKRG RAQTAPTKTS PRNAKKHDEL WHDGVCPSVA NPLEVYLIPT PPENITFEDP
SLDVILLLRV LHAISRYWYY LYDNAMCKEI IPTSEFINSK LTAKANRQLQ DPLVIMTGNI
PTWLTELGKT CPFFFPFDTR QMLFYVTAFD RDRAMQRLLD TNPEINQSDS QDSRVAPRLD
RKKRTVNREE LLKQAESVMQ DLGSSRAMLE IQYENEVGTG LGPTLEFYAL VSQELQRADL
GLWRGEEVTL SNPKGSQEGT KYIQNLQGLF ALPFGRTAKP AHIAKVKMKF RFLGKLMAKA
IMDFRLVDLP LGLPFYKWML RQETSLTSHD LFDIDPVVAR SVYHLEDIVR QKKRLEQDKS
QTKESLQYAL ETLTMNGCSV EDLGLDFTLP GFPNIELKKG GKDIPVTIHN LEEYLRLVIF
WALNEGVCRQ FDSFRDGFES VFPLSHLQYF YPEELDQLLC GSKADTWDAK TLMECCRPDH
GYTHDSRAVK FLFEILSSFD NEQQRLFLQF VTGSPRLPVG GFRSLNPPLT IVRKTFESTE
NPDDFLPSVM TCVNYLKLPD YSSIEIMRDK LLIAAREGQQ SFHLS
