UBR4_RAT
ID UBR4_RAT Reviewed; 5194 AA.
AC Q2TL32; Q5BJM4;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 23-FEB-2022, entry version 113.
DE RecName: Full=E3 ubiquitin-protein ligase UBR4;
DE EC=2.3.2.27;
DE AltName: Full=N-recognin-4;
DE AltName: Full=RING-type E3 ubiquitin transferase UBR4;
DE AltName: Full=Zinc finger UBR1-type protein 1;
GN Name=Ubr4; Synonyms=Rbaf600, Zubr1;
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 [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Retina;
RA Zhang Q., Anderson R.E.;
RT "Expression and characterization of a zinc-finger containing gene (ZUBR1)
RT induced by bright cyclic light.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4841-5194.
RC TISSUE=Spleen;
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-1403, 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; SER-181; SER-1755;
RP SER-2719; SER-2722 AND THR-2724, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 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. Together
CC with clathrin, forms meshwork structures involved in membrane
CC morphogenesis and cytoskeletal organization. Regulates integrin-
CC mediated signaling. May play a role in activation of FAK in response to
CC cell-matrix interactions. Mediates ubiquitination of ACLY, leading to
CC its subsequent degradation (By similarity). {ECO:0000250}.
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 RB1 and calmodulin. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Nucleus {ECO:0000250}. Note=Concentrates at the leading
CC edge of membrane structures involved in actin motility. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the UBR4 family. {ECO:0000305}.
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DR EMBL; AY850927; AAX45146.1; -; mRNA.
DR EMBL; BC091421; AAH91421.1; -; mRNA.
DR RefSeq; NP_001034115.1; NM_001039026.1.
DR BioGRID; 260504; 4.
DR IntAct; Q2TL32; 2.
DR MINT; Q2TL32; -.
DR STRING; 10116.ENSRNOP00000032156; -.
DR CarbonylDB; Q2TL32; -.
DR iPTMnet; Q2TL32; -.
DR PhosphoSitePlus; Q2TL32; -.
DR jPOST; Q2TL32; -.
DR PaxDb; Q2TL32; -.
DR PRIDE; Q2TL32; -.
DR GeneID; 313658; -.
DR KEGG; rno:313658; -.
DR UCSC; RGD:1563121; rat.
DR CTD; 23352; -.
DR RGD; 1563121; Ubr4.
DR eggNOG; KOG1776; Eukaryota.
DR InParanoid; Q2TL32; -.
DR OrthoDB; 717at2759; -.
DR PhylomeDB; Q2TL32; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q2TL32; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR025704; E3_Ub_ligase_UBR4_C.
DR InterPro; IPR045841; E3_UBR4_N.
DR InterPro; IPR045189; UBR4-like.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR21725; PTHR21725; 1.
DR Pfam; PF13764; E3_UbLigase_R4; 1.
DR Pfam; PF19423; E3_UBR4_N; 1.
DR Pfam; PF02207; zf-UBR; 1.
DR SMART; SM00396; ZnF_UBR1; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS51157; ZF_UBR; 1.
PE 1: Evidence at protein level;
KW Acetylation; Calmodulin-binding; Cytoplasm; Cytoskeleton; Membrane;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..5194
FT /note="E3 ubiquitin-protein ligase UBR4"
FT /id="PRO_0000286863"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 408..428
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 1657..1730
FT /note="UBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00508"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2431..2468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2711..2764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2875..2979
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3357..3396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..586
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..621
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2445..2468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2875..2903
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2941..2961
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2962..2979
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3357..3376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3377..3396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2AN08"
FT MOD_RES 370
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:A2AN08"
FT MOD_RES 1085
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q5T4S7"
FT MOD_RES 1403
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 1648
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T4S7"
FT MOD_RES 1653
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T4S7"
FT MOD_RES 1748
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T4S7"
FT MOD_RES 1755
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1878
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T4S7"
FT MOD_RES 1904
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T4S7"
FT MOD_RES 2715
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5T4S7"
FT MOD_RES 2719
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2722
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2724
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2956
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5T4S7"
FT MOD_RES 2964
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T4S7"
SQ SEQUENCE 5194 AA; 573792 MW; 1F7C929C147369E5 CRC64;
MATSGGEEAA AAAPAPGAPA TGQDTTPGWE VAVRPLLSAS YSAFEMKELP QLVASVIESE
SEILHHEKQY EPFYSSFVAL STHYITTVCS LIPRNQLQSV AAACKVLIEF SLLRLENPDE
ACAVSQKHLI LLIKGLCTGC SRLDRTEIIT FTAMMKSAKL PQTVKTLSDV EDQKELASPV
SPELRQKEVQ MNFLNQLTSV FNPRTVPSPP ISPQALVEGE NDEQSSTEQA SAVKTKNVFI
AQNVASLQEL GGSEKLLRVC LNLPYFLRYI NRFQDAVVAN SFFIMPATVA DATAVRNGFH
SLVIDVTMAL DTLSLPVLEP LNPSRLQDVT VLSLSCLYAG VSVATCMAIL HVGSAQQVRT
GSTSSKEEDY ESDAATIVQK CLEIYDMIGQ AISSSRRAGG EHFQNFQLLG AWCLLNSLFL
ILHLSPTALA DKGKEKDPLA ALRVRDILSR TKEGVGSPKL GPGKGHQGFG VLSVILANHA
IKLLTSLFQD LQVEALHKGW ETDGPPAVLS IMAQSTSTQR VQRLIDSVPL TNLLLTLLST
SYRKACVLQR QRKGSMSSDA SASTDSNTYY EDDFSSTEED SSQDDDSEPI LGQWFEETIS
PSKEKAAPPP PPPPPPLESS PRVKSPSKQA SGEKGNILAS RKDPELFLGL ASNILNFITS
SMLNSRNNFI RNYLSVSLSE QHMATLASII KEVDKDGLKG SSDEDFAAAL YHFNHSLVTS
DLQSPNLQNT LLQQLGVAPL SSGPWPLYIH PQGLSVLSRL LLIWQHKAGA QGDPDVPECL
KVWDRFLTTM KQSALQGVVP SETEDLNIEH LQLLLLIFHS FSEKGRRAIL TTLVQSIQEL
SVNMEVQMRS APLILARLLL IFDYLLHQYS KAPVYLFEQV QHNLLSPPFG WASGSQDSSS
SSRRANIPLY HGFKEVEENW SKHFSSDAAP QPRFYCVLST EASEEDLNRL DSEACEVLFS
KLVKYDELYS SLTALLAAGS QLDTVKRKEN KNMTALEACA LQYYFLILWR ILGILPPSKT
YMNQLAMNSP EMSECDILHT LRWSSRLRIS SYVSWIKDHL IRQGMRPEHA GSLVELAASK
CSSVKYDVEI VEEYFARQIS SFCSIDCTTV LQLHEIPSLQ SIYTLDAAVS KVQVSLDEHF
SKMAAETDPH KSSEITKNLL PATLQLIDTY ASFTRAYLLQ NLNEEGSTEK PSQEKLHGFA
AVLAIGSSRC KANTLGPTLV QNLPSSVQSV CESWNNINTN EFPNIGSWRN AFANDTIPSE
SYISAVQAAH LGTLCGQSLP LAASLKHALL SLVRLTGDLI VWSDEMNPAQ VIRALLPLLL
ESSTESAAEI SSNSLERILG PAESDEFLAR VYEKLITGCY NILANHADPS SGLDESVLEE
CLQYLEKQLE SSQARKAMEE FFSDGGELVQ IMMATANEDL SAKFCNRVLK FFTKLFQLTE
KSPNPSLLHL CGSLAQLACV EPVRLQAWLT RMTTSPPKDS DQLEVIQENR QLLQLLTTYI
VRENSQVGEG VCAVLLGTLT PMATDMLANG DGTGFPELMV VMATLASAGQ GAGHLQLHNA
AVDWLGRCKK YLSQKNVVEK LNANVMHGKH VMVLECTCHI MSYLADVTNA LSQSNGQGPS
HLSVDGEERA IEVDSDWVEE LAVEEEDSQA EDSDEDSLCN KLCTFTITQK EFMNQHWYHC
HTCKMVDGVG VCTVCAKVCH KDHEISYAKY GSFFCDCGAK EDGSCLALVK RTPSSGMSST
MKESAFQSEP RVSESLVRHA STSPADKAKV TISDGKVADE EKPKKSSLCR TVEGCREELQ
NQANFSFAPL VLDMLNFLMD AIQTNFQQAS AVGSSSRAQQ ALSELHTVDK VVEMTDQLMV
PTLGSQEGAF ENVRMNYSGD QGQTIRQLIS AHVLRRVAMC VLSSPHGRRQ HLAVSHEKGK
ITVLQLSALL KQADSSKRKL TLTRLASAPV PFTVLSLTGN PCKEDYLAVC GLKDCHVLTF
SSSGSVSDHL VLHPQLATGN FIIKAVWLPG SQTELAIVTA DFVKIYDLSV DALSPTFYFL
LPSSKIRDVT FLFNEEGKNI IVIMSSAGYM YTQLMEEASS AQQGPFYVTN VLEINHEDLK
DSNSQVAGGG VSVYYSHVLQ MLFFSYSQGK SFAATVSRST LEVLQLFPIN IKSSNGGSKT
SPALCQWSEV MNHPGLVCCV QQTTGVPLVV MVKPDTFLIQ EIKTLPAKAK IQDMVAIRHT
ACNEQQRTTM ILLCEDGSLR IYMANVENTS YWLQPSLQPS SVISIMKPVR KRKTATITAR
TSSQVTFPID FFEHNQQLTD VEFGGNDLLQ VYNAQQIKHR LNSTGMYVAN TKPGGFTMEI
SNNSSTMVMT GMRIQIGTQA IERAPSYIEI FGRTMQLNLS RSRWFDFPFT REEALQADRK
LNLFIGASVD PAGVTMIDAV KIYGKTKEQF GWPDEPPEDF PSASVSSVCP PNLNQSNSTG
DSDSAAPATT SGTVLERLVV SSLEALESCF AVGPIIEKER NKHAAQELAT LLLSLPAPAS
VQQQSKSLLA SLHSSRSAYH SHKDQALLSK AVQCLNTSSK EGKDLDPEVF QRLVITARSI
AVTRPNNLVH FTESKLPQME TEGAEEGKEP QKQVEGDGCS FITQLVNHFW KLHASKPKNA
FLAPACLPGL THIEATVNAL VDIIHGYCTC ELDCINTASK IYMQMLLCPD PAVSFSCKQA
LIRVLRPRNK RRHVTLPSSP RSNTPMGDKD DDDDDDADEK MQSSGIPDGG HIRQESQEQS
EVDHGDFEMV SESMVLETAE NVNNGNPSPL EALLAGAEGF PPMLDIPPDA DDETMVELAI
ALSLQQDQQG SSSSALGLQS LGLSGQAPSS SSLDAGTLSD TTASGVCACN SSVTLSAPAS
DDEGSTAATD GSTLRTSPAD HGGSVGSESG GSAVDSVAGE HSVSGRSSAY GDATAEGHPA
GPGSVSSSTG AISTTTGHQE GDGSEGEGEG EAEGDVHTSN RLHMVRLMLL ERLLQTLPQL
RNVGGVRAIP YMQVILMLTT DLDGEDEKDK GALDNLLAQL IAELGMDKKD VSKKNERSAL
NEVHLVVMRL LSVFMSRTKS GSKSSICESS SLISSATAAA LLSSGAVDYC LHVLKSLLEY
WKGQQSEEEP VTTSQLLKPH TTSSPPDMSP FFLRQYVKGH AADVFEAYTQ LLTEMVLRLP
YQIKKIADTS SRIPPPVFDH SWFYFLSEYL MIQQTPFVRR QVRKLLLFIC GSKEKYRQLR
DLHTLDSHVR GIKKLLEEQG IFLRASVVTA SSGSALQYDT LISLMEHLKA CAEIAAQRTI
NWQKFCIKDD SVLYFLLQVS FLVDEGVSPV LLQLLSCALC GSKVLAALAA STGSSSVASS
APPAASSGQT TTQSKSSTKK SKKEKKEKEK EGESSGSQED QLCTALVNQL NRFADKETLI
QFLRCFLLES NSSSVRWQAH CLTLHIYRNS NKAQQELLLD LMWSIWPELP AYGRKAAQFV
DLLGYFSLKT AQTEKKLKEY SQKAVEILRT QNHILTNHPN SNIYNTLSGL VEFDGYYLES
DPCLVCNNPE VPFCYIKLSS IKVDTRYTTT QQVVKLIGSH TISKVTVKIG DLKRTKMVRT
INLYYNNRTV QAIVELKNKP ARWHKAKKVQ LTPGQTEVKI DLPLPIVASN LMIEFADFYE
NYQASTETLQ CPRCSASVPA NPGVCGNCGE NVYQCHKCRS INYDEKDPFL CNACGFCKYA
RFDFMLYAKP CCAVDPIENE EDRKKAVSNI NTLLDKADRV YHQLMGHRPQ LENLLCKVNE
AAPEKPQEDS GTAGGISSTS ASVNRYILQL AQEYCGDCKN SFDELSKIIQ KVFASRKELL
EYDLQQREAA TKSSRTSVQP TFTASQYRAL SVLGCGHTSS TKCYGCASAV TEHCITLLRA
LATNPALRHI LVSQGLIREL FDYNLRRGAA AIREEVRQLM CLLTRDNPEA TQQMNDLIIG
KVSTALKGHW ANPDLASSLQ YEMLLLTDSI SKEDSCWELR LRCALSLFLM AVNIKTPVVV
ENITLMCLRI LQKLIKPPAP TSKKNKDVPV EALTTVKPYC NEIHAQAQLW LKRDPKASYE
AWKKCLPIRG VDGNGKSPSK SELHRLYLTE KYVWRWKQFL SRRGKRTTPL DLKLGHNNWL
RQVLFTPATQ AARQAACTIV EALASVPSRK QQVLDLLTSY LDELSVAGEC AAEYLALYQK
LIASCHWKVY LAARGVLPYV GNLITKEIAR LLALEEATLS TDLQQGYALK SLTGLLSSFV
EVESIKRHFK SRLVGTVLNG YLCLRKLVLQ RTKLIDETQD MLLEMLEDMT TGTESETKAF
MAVCIETAKR YNLDDYRTPV FIFERLCSII YPEENEVTEF FVTLEKDPQQ EDFLQGRMPG
NPYSSNEPGI GPLMRDIKNK ICQDCDLVAL LEDDSGMELL VNNKIISLDL PVAEVYKKVW
CTTNEGEPMR IVYRMRGLLG DATEEFIESL DSTTDEEEDE EEVYRMAGVM AQCGGLQCML
NRLAGVKDFK QGRHLLTVLL KLFSYCVKVK VNRQQLVKLE MNTLNVMLGT LNLALVAEQE
SKDSGGAAVA EQVLSIMEII LDESNAEPLS EDKGNLLLTG DKDQLVMLLD QINSTFVRSN
PSVLQGLLRI IPYLSFGEVE KMQILVERFK PYCSFDKYDE DHSGDDKVFL DCFCKIAAGI
KNNSNGHQLK DLILQKGITQ SALDYMKKHI PSAKNLDADI WKKFLSRPAL PFILRLLRGL
AMQHPATQVL IGTDSITSLH KLEQVSSDEG IGTLAENLLE ALREHPDVNK KIDAARRETR
AEKKRMAMAM RQKALGTLGM TTNEKGQVVT KTALLKQMEE LIEEPGLTCC ICREGYKFQP
TKVLGIYTFT KRVALEEMEN KPRKQQGYST VSHFNIVHYD CHLAAVRLAR GREEWESAAL
QNANTKCNGL LPVWGPHVPE SAFATCLARH NTYLQECTGQ REPTYQLNIH DIKLLFLRFA
MEQSFSADTG GGGRESNIHL IPYIIHTVLY VLNTTRATSR EEKNLQGFLE QPREKWTESA
FDVDGPHYFT ILALHVLPPE QWKATRVEIL RRLLVASHAR AVAPGGATRL TDKAVKDYSA
YRSSLLFWAL VDLIYNMFKK VPTSNTEGGW SCSLAEYIRH NDMPIYEAAD KALKTFQEEF
MPVETFSEFL DAAGLLSEIT DPESFLKDLL NSVP
