UBR1_MOUSE
ID UBR1_MOUSE Reviewed; 1757 AA.
AC O70481; A2AQ54; Q5BKR8; Q792M3; Q8BN40; Q8C5K3;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=E3 ubiquitin-protein ligase UBR1;
DE EC=2.3.2.27;
DE AltName: Full=N-recognin-1;
DE AltName: Full=RING-type E3 ubiquitin transferase UBR1;
DE AltName: Full=Ubiquitin-protein ligase E3-alpha-1;
DE AltName: Full=Ubiquitin-protein ligase E3-alpha-I;
GN Name=Ubr1;
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 [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=129/SvJ;
RX PubMed=9653112; DOI=10.1073/pnas.95.14.7898;
RA Kwon Y.T., Reiss Y., Fried V.A., Hershko A., Yoon J.K., Gonda D.K.,
RA Sangan P., Copeland N.G., Jenkins N.A., Varshavsky A.;
RT "The mouse and human genes encoding the recognition component of the N-end
RT rule pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:7898-7903(1998).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-849 AND 1529-1757.
RC STRAIN=NOD; TISSUE=Olfactory bulb, and Spleen;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-852.
RC STRAIN=C57BL/6J; TISSUE=Brain;
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, AND FUNCTION.
RX PubMed=11689692; DOI=10.1128/mcb.21.23.8007-8021.2001;
RA Kwon Y.T., Xia Z., Davydov I.V., Lecker S.H., Varshavsky A.;
RT "Construction and analysis of mouse strains lacking the ubiquitin ligase
RT UBR1 (E3alpha) of the N-end rule pathway.";
RL Mol. Cell. Biol. 21:8007-8021(2001).
RN [6]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=14585983; DOI=10.1128/mcb.23.22.8255-8271.2003;
RA Kwon Y.T., Xia Z., An J.Y., Tasaki T., Davydov I.V., Seo J.W., Sheng J.,
RA Xie Y., Varshavsky A.;
RT "Female lethality and apoptosis of spermatocytes in mice lacking the UBR2
RT ubiquitin ligase of the N-end rule pathway.";
RL Mol. Cell. Biol. 23:8255-8271(2003).
RN [7]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15548684; DOI=10.1158/0008-5472.can-04-2102;
RA Kwak K.S., Zhou X., Solomon V., Baracos V.E., Davis J., Bannon A.W.,
RA Boyle W.J., Lacey D.L., Han H.Q.;
RT "Regulation of protein catabolism by muscle-specific and cytokine-inducible
RT ubiquitin ligase E3alpha-II during cancer cachexia.";
RL Cancer Res. 64:8193-8198(2004).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=16311597; DOI=10.1038/ng1681;
RA Zenker M., Mayerle J., Lerch M.M., Tagariello A., Zerres K., Durie P.R.,
RA Beier M., Hulskamp G., Guzman C., Rehder H., Beemer F.A., Hamel B.C.J.,
RA Vanlieferinghen P., Gershoni-Baruch R., Vieira M.W., Dumic M.,
RA Auslender R., Gil-da-Silva-Lopes V.L., Steinlicht S., Rauh M., Shalev S.A.,
RA Thiel C., Winterpacht A., Kwon Y.T., Varshavsky A., Reis A.;
RT "Deficiency of UBR1, a ubiquitin ligase of the N-end rule pathway, causes
RT pancreatic dysfunction, malformations and mental retardation (Johanson-
RT Blizzard syndrome).";
RL Nat. Genet. 37:1345-1350(2005).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=16606826; DOI=10.1073/pnas.0601700103;
RA An J.Y., Seo J.W., Tasaki T., Lee M.J., Varshavsky A., Kwon Y.T.;
RT "Impaired neurogenesis and cardiovascular development in mice lacking the
RT E3 ubiquitin ligases UBR1 and UBR2 of the N-end rule pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6212-6217(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC 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: E3 ubiquitin-protein ligase which is a component of the N-end
CC rule pathway. Recognizes and binds to proteins bearing specific N-
CC terminal residues that are destabilizing according to the N-end rule,
CC leading to their ubiquitination and subsequent degradation. May be
CC involved in pancreatic homeostasis. Binds leucine and is a negative
CC regulator of the leucine-mTOR signaling pathway, thereby controlling
CC cell growth (By similarity). {ECO:0000250, ECO:0000269|PubMed:11689692,
CC ECO:0000269|PubMed:14585983, ECO:0000269|PubMed:16311597}.
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=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with RECQL4. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Present in skeletal muscle and liver (at protein
CC level). Broadly expressed, with highest levels in skeletal muscle and
CC heart. Expressed in acinar cells of the pancreas. In testes, expressed
CC primarily in spermatogonia. {ECO:0000269|PubMed:11689692,
CC ECO:0000269|PubMed:14585983, ECO:0000269|PubMed:15548684,
CC ECO:0000269|PubMed:16311597, ECO:0000269|PubMed:9653112}.
CC -!- DEVELOPMENTAL STAGE: Expressed in limb buds at 9.5-11.5 dpc.
CC {ECO:0000269|PubMed:9653112}.
CC -!- INDUCTION: In models of cancer cachexia, induced in muscle during the
CC progression of wasting. {ECO:0000269|PubMed:15548684}.
CC -!- DOMAIN: The RING-H2 zinc finger is an atypical RING finger with a His
CC ligand in place of the fourth Cys of the classical motif.
CC -!- DOMAIN: The UBR-type zinc finger forms a pocket that mediates
CC recognition of type 1 N-degrons. It exhibits preference for Arginine in
CC first position, has poor affinity for histidine, and doesn't bind
CC acetylated peptides (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable and fertile, but show a decreased
CC mass of skeletal muscle and adipose tissue. They have exocrine
CC pancreatic insufficiency with impaired stimulus-secretion coupling and
CC increased susceptibiliy to pancreatic injury. UBR1 and UBR2 double
CC knockout embryos die at midgestation, with defects in neurogenesis and
CC cardiovascular development. These defects included reduced
CC proliferation as well as precocious migration and differentiation of
CC neural progenitor cells. {ECO:0000269|PubMed:16311597,
CC ECO:0000269|PubMed:16606826}.
CC -!- SIMILARITY: Belongs to the UBR1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH90969.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AF061555; AAC40165.1; -; mRNA.
DR EMBL; AH006182; AAC23678.1; -; Genomic_DNA.
DR EMBL; AL844548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL935168; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK078173; BAC37160.1; -; mRNA.
DR EMBL; AK089616; BAC40933.1; -; mRNA.
DR EMBL; BC090969; AAH90969.1; ALT_SEQ; mRNA.
DR CCDS; CCDS16628.1; -.
DR PIR; T14318; T14318.
DR RefSeq; NP_033487.2; NM_009461.2.
DR AlphaFoldDB; O70481; -.
DR SMR; O70481; -.
DR BioGRID; 204422; 9.
DR ELM; O70481; -.
DR IntAct; O70481; 2.
DR STRING; 10090.ENSMUSP00000028728; -.
DR iPTMnet; O70481; -.
DR PhosphoSitePlus; O70481; -.
DR EPD; O70481; -.
DR MaxQB; O70481; -.
DR PaxDb; O70481; -.
DR PeptideAtlas; O70481; -.
DR PRIDE; O70481; -.
DR ProteomicsDB; 297797; -.
DR Antibodypedia; 23750; 204 antibodies from 28 providers.
DR DNASU; 22222; -.
DR Ensembl; ENSMUST00000028728; ENSMUSP00000028728; ENSMUSG00000027272.
DR GeneID; 22222; -.
DR KEGG; mmu:22222; -.
DR UCSC; uc008lxb.1; mouse.
DR CTD; 197131; -.
DR MGI; MGI:1277977; Ubr1.
DR VEuPathDB; HostDB:ENSMUSG00000027272; -.
DR eggNOG; KOG1140; Eukaryota.
DR GeneTree; ENSGT00950000183075; -.
DR HOGENOM; CLU_001801_2_0_1; -.
DR InParanoid; O70481; -.
DR OMA; ATTVYRI; -.
DR OrthoDB; 81415at2759; -.
DR PhylomeDB; O70481; -.
DR TreeFam; TF323875; -.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 22222; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Ubr1; mouse.
DR PRO; PR:O70481; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; O70481; protein.
DR Bgee; ENSMUSG00000027272; Expressed in ascending aorta and 245 other tissues.
DR Genevisible; O70481; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0000502; C:proteasome complex; IGI:MGI.
DR GO; GO:0000151; C:ubiquitin ligase complex; IGI:MGI.
DR GO; GO:0070728; F:leucine binding; ISO:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071233; P:cellular response to leucine; ISS:UniProtKB.
DR GO; GO:0032007; P:negative regulation of TOR signaling; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:MGI.
DR GO; GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; IBA:GO_Central.
DR Gene3D; 3.30.1390.10; -; 1.
DR InterPro; IPR003769; ClpS_core.
DR InterPro; IPR044046; E3_ligase_UBR-like_C.
DR InterPro; IPR014719; Ribosomal_L7/12_C/ClpS-like.
DR InterPro; IPR039164; UBR1-like.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR21497; PTHR21497; 1.
DR Pfam; PF02617; ClpS; 1.
DR Pfam; PF18995; PRT6_C; 1.
DR Pfam; PF02207; zf-UBR; 1.
DR SMART; SM00396; ZnF_UBR1; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF54736; SSF54736; 1.
DR PROSITE; PS51157; ZF_UBR; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Metal-binding; Phosphoprotein; Reference proteome;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8IWV7"
FT CHAIN 2..1757
FT /note="E3 ubiquitin-protein ligase UBR1"
FT /id="PRO_0000056137"
FT ZN_FING 97..168
FT /note="UBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00508"
FT ZN_FING 1101..1204
FT /note="RING-type; atypical"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..861
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWV7"
FT MOD_RES 1182
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWV7"
FT CONFLICT 639
FT /note="G -> S (in Ref. 1; AAC40165 and 3; BAC40933)"
FT /evidence="ECO:0000305"
FT CONFLICT 888
FT /note="M -> I (in Ref. 1; AAC40165)"
FT /evidence="ECO:0000305"
FT CONFLICT 901
FT /note="M -> T (in Ref. 1; AAC40165)"
FT /evidence="ECO:0000305"
FT CONFLICT 964
FT /note="K -> R (in Ref. 1; AAC40165)"
FT /evidence="ECO:0000305"
FT CONFLICT 973
FT /note="S -> G (in Ref. 1; AAC40165)"
FT /evidence="ECO:0000305"
FT CONFLICT 1008
FT /note="V -> I (in Ref. 1; AAC40165)"
FT /evidence="ECO:0000305"
FT CONFLICT 1357
FT /note="N -> S (in Ref. 1; AAC40165)"
FT /evidence="ECO:0000305"
FT CONFLICT 1371
FT /note="T -> A (in Ref. 1; AAC40165)"
FT /evidence="ECO:0000305"
FT CONFLICT 1464
FT /note="S -> P (in Ref. 1; AAC40165)"
FT /evidence="ECO:0000305"
FT CONFLICT 1496
FT /note="A -> T (in Ref. 1; AAC40165)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1757 AA; 200240 MW; 935C0531A5F25A66 CRC64;
MADEEMDGAE RMDVSPEPPL APQRPASWWD QQVDFYTAFL HHLAQLVPEI YFAEMDPDLE
KQEESVQMSI LTPLEWYLFG EDPDICLEKL KHSGAFQLCG KVFKSGETTY SCRDCAIDPT
CVLCMDCFQS SVHKNHRYKM HTSTGGGFCD CGDTEAWKTG PFCVDHEPGR AGTTKESLHC
PLNEEVIAQA RRIFPSVIKY IVEMTIWEEE KELPPELQIR EKNERYYCVL FNDEHHSYDH
VIYSLQRALD CELAEAQLHT TAIDKEGRRA VKAGVYATCQ EAKEDIKSHS ENVSQHPLHV
EVLHSVVMAH QKFALRLGSW MNKIMSYSSD FRQIFCQACL VEEPGSENPC LISRLMLWDA
KLYKGARKIL HELIFSSFFM EMEYKKLFAM EFVKYYKQLQ KEYISDDHER SISITALSVQ
MLTVPTLARH LIEEQNVISV ITETLLEVLP EYLDRNNKFN FQGYSQDKLG RVYAVICDLK
YILISKPVIW TERLRAQFLE GFRSFLKILT CMQGMEEIRR QVGQHIEVDP DWEAAIAIQM
QLKNILLMFQ EWCACDEDLL LVAYKECHKA VMRCSTNFMS STKTVVQLCG HSLETKSYKV
SEDLVSIHLP LSRTLAGLHV RLSRLGAISR LHEFVPFDGF QVEVLVEYPL RCLVLVAQVV
AEMWRRNGLS LISQVFYYQD VKCREEMYDK DIIMLQIGAS IMDPNKFLLL VLQRYELTDA
FNKTISTKDQ DLIKQYNTLI EEMLQVLIYI VGERYVPGVG NVTREEVIMR EITHLLCIEP
MPHSAIARNL PENENNETGL ENVINKVATF KKPGVSGHGV YELKDESLKD FNMYFYHYSK
TQHSKAEHMQ KKRRKQENKD EALPPPPPPE FCPAFSKVVN LLSCDVMMYI LRTIFERAVD
MESNLWTEGM LQMAFHILAL GLLEEKQQLQ KAPEEEVAFD FYHKASRLGS SAMNAQNIQM
LLEKLKGIPQ LESQKDMITW ILQMFDTVKR LREKSCLVVA TTSGLECVKS EEITHDKEKA
ERKRKAEAAR LHRQKIMAQM SALQKNFIET HKLMYDNTSE VTGKEDSIME EESTSAVSEA
SRIALGPKRG PAVTEKEVLT CILCQEEQEV KLENNAMVLS ACVQKSTALT QHRGKPVDHL
GETLDPLFMD PDLAHGTYTG SCGHVMHAVC WQKYFEAVQL SSQQRIHVDL FDLESGEYLC
PLCKSLCNTV IPIIPLQPQK INSENAEALA QLLTLARWIQ TVLARISGYN IKHAKGEAPA
VPVLFNQGMG DSTFEFHSIL SFGVQSSVKY SNSIKEMVIL FATTIYRIGL KVPPDELDPR
VPMMTWSTCA FTIQAIENLL GDEGKPLFGA LQNRQHNGLK ALMQFAVAQR TTCPQVLIHK
HLARLLSVIL PNLQSENTPG LLSVDLFHVL VGAVLAFPSL YWDDTVDLQP SPLSSSYNHL
YLFHLITMAH MLQILLTTDT DLSSGPPLAE GEEDSEEARC ASAFFVEVSQ HTDGLAGCGA
PGWYLWLSLR NGITPYLRCA ALLFHYLLGV APPEELFANS AEGEFSALCS YLSLPTNLFL
LFQEYWDTIR PLLQRWCGDP ALLKSLKQKS AVVRYPRKRN SLIELPEDYS CLLNQASHFR
CPRSADDERK HPVLCLFCGA ILCSQNICCQ EIVNGEEVGA CVFHALHCGA GVCIFLKIRE
CRVVLVEGKA RGCAYPAPYL DEYGETDPGL KRGNPLHLSR ERYRKLHLVW QQHCIIEEIA
RSQETNQMLF GFNWQLL
