UBR3_HUMAN
ID UBR3_HUMAN Reviewed; 1888 AA.
AC Q6ZT12; B4DZR7; Q2KHN5; Q6ZR55; Q6ZSC2; Q8IVE7; Q8ND96;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=E3 ubiquitin-protein ligase UBR3;
DE EC=2.3.2.27;
DE AltName: Full=N-recognin-3;
DE AltName: Full=RING-type E3 ubiquitin transferase UBR3;
DE AltName: Full=Ubiquitin-protein ligase E3-alpha-3;
DE AltName: Full=Ubiquitin-protein ligase E3-alpha-III;
DE AltName: Full=Zinc finger protein 650;
GN Name=UBR3; Synonyms=KIAA2024, ZNF650;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RA Nagase T., Kikuno R., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1092-1888 (ISOFORM 1), AND NUCLEOTIDE SEQUENCE [LARGE
RP SCALE MRNA] OF 1330-1888 (ISOFORM 4).
RC TISSUE=Brain, Testis, Tongue, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1432-1888 (ISOFORMS 1/2).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP FUNCTION.
RX PubMed=27331610; DOI=10.7554/elife.15258;
RA Li T., Giagtzoglou N., Eberl D.F., Jaiswal S.N., Cai T., Godt D.,
RA Groves A.K., Bellen H.J.;
RT "The E3 ligase Ubr3 regulates Usher syndrome and MYH9 disorder proteins in
RT the auditory organs of Drosophila and mammals.";
RL Elife 5:E15258-E15258(2016).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which is a component of the N-end
CC rule pathway (By similarity). Does not bind to proteins bearing
CC specific N-terminal residues that are destabilizing according to the N-
CC end rule, leading to their ubiquitination and subsequent degradation
CC (By similarity). May play a role in Shh signaling by mediating the
CC ubiquitination of Kif7 (By similarity). May be important for MYH9
CC function in certain tissues, possibly by regulating the ubiquitination
CC of MYH9 and consequently affecting its interaction with MYO7A
CC (PubMed:27331610). {ECO:0000250|UniProtKB:Q5U430,
CC ECO:0000269|PubMed:27331610}.
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 UBE2A and UBE2B.
CC {ECO:0000250|UniProtKB:Q5U430}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6ZT12-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZT12-2; Sequence=VSP_030354, VSP_023142;
CC Name=3;
CC IsoId=Q6ZT12-3; Sequence=VSP_023141;
CC Name=4;
CC IsoId=Q6ZT12-4; Sequence=VSP_036405;
CC -!- SIMILARITY: Belongs to the UBR1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC23120.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC86783.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC87032.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAG64179.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAD38857.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB095944; BAC23120.1; ALT_INIT; mRNA.
DR EMBL; AK126998; BAC86783.1; ALT_INIT; mRNA.
DR EMBL; AK127553; BAC87032.1; ALT_INIT; mRNA.
DR EMBL; AK128490; BAC87462.1; -; mRNA.
DR EMBL; AK303062; BAG64179.1; ALT_INIT; mRNA.
DR EMBL; AC009967; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079151; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092641; AAY14890.1; -; Genomic_DNA.
DR EMBL; AL834144; CAD38857.1; ALT_SEQ; mRNA.
DR CCDS; CCDS2238.2; -. [Q6ZT12-1]
DR RefSeq; NP_742067.3; NM_172070.3. [Q6ZT12-1]
DR AlphaFoldDB; Q6ZT12; -.
DR SMR; Q6ZT12; -.
DR BioGRID; 126237; 114.
DR IntAct; Q6ZT12; 32.
DR MINT; Q6ZT12; -.
DR STRING; 9606.ENSP00000396068; -.
DR GlyGen; Q6ZT12; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6ZT12; -.
DR PhosphoSitePlus; Q6ZT12; -.
DR BioMuta; UBR3; -.
DR DMDM; 166214992; -.
DR EPD; Q6ZT12; -.
DR jPOST; Q6ZT12; -.
DR MassIVE; Q6ZT12; -.
DR MaxQB; Q6ZT12; -.
DR PaxDb; Q6ZT12; -.
DR PeptideAtlas; Q6ZT12; -.
DR PRIDE; Q6ZT12; -.
DR ProteomicsDB; 68252; -. [Q6ZT12-1]
DR ProteomicsDB; 68253; -. [Q6ZT12-2]
DR ProteomicsDB; 68254; -. [Q6ZT12-3]
DR ProteomicsDB; 68255; -. [Q6ZT12-4]
DR Antibodypedia; 33822; 43 antibodies from 14 providers.
DR DNASU; 130507; -.
DR Ensembl; ENST00000272793.11; ENSP00000272793.5; ENSG00000144357.18. [Q6ZT12-1]
DR GeneID; 130507; -.
DR KEGG; hsa:130507; -.
DR MANE-Select; ENST00000272793.11; ENSP00000272793.5; NM_172070.4; NP_742067.3.
DR UCSC; uc010zdi.3; human. [Q6ZT12-1]
DR CTD; 130507; -.
DR DisGeNET; 130507; -.
DR GeneCards; UBR3; -.
DR HGNC; HGNC:30467; UBR3.
DR HPA; ENSG00000144357; Tissue enhanced (skeletal muscle, tongue).
DR MIM; 613831; gene.
DR neXtProt; NX_Q6ZT12; -.
DR OpenTargets; ENSG00000144357; -.
DR PharmGKB; PA162407919; -.
DR VEuPathDB; HostDB:ENSG00000144357; -.
DR eggNOG; KOG1139; Eukaryota.
DR GeneTree; ENSGT00950000183075; -.
DR HOGENOM; CLU_000651_2_1_1; -.
DR InParanoid; Q6ZT12; -.
DR OMA; GNKDELH; -.
DR OrthoDB; 81415at2759; -.
DR PhylomeDB; Q6ZT12; -.
DR TreeFam; TF323875; -.
DR PathwayCommons; Q6ZT12; -.
DR SignaLink; Q6ZT12; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 130507; 11 hits in 1119 CRISPR screens.
DR ChiTaRS; UBR3; human.
DR GenomeRNAi; 130507; -.
DR Pharos; Q6ZT12; Tbio.
DR PRO; PR:Q6ZT12; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q6ZT12; protein.
DR Bgee; ENSG00000144357; Expressed in vastus lateralis and 188 other tissues.
DR ExpressionAtlas; Q6ZT12; baseline and differential.
DR Genevisible; Q6ZT12; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0007608; P:sensory perception of smell; ISS:UniProtKB.
DR GO; GO:0001967; P:suckling behavior; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; IBA:GO_Central.
DR InterPro; IPR044046; E3_ligase_UBR-like_C.
DR InterPro; IPR039164; UBR1-like.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR21497; PTHR21497; 1.
DR Pfam; PF18995; PRT6_C; 1.
DR Pfam; PF02207; zf-UBR; 1.
DR SMART; SM00396; ZnF_UBR1; 1.
DR PROSITE; PS51157; ZF_UBR; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Coiled coil; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1888
FT /note="E3 ubiquitin-protein ligase UBR3"
FT /id="PRO_0000278184"
FT TRANSMEM 761..781
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 919..939
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1806..1826
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 118..189
FT /note="UBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00508"
FT ZN_FING 1306..1364
FT /note="RING-type; degenerate"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1008..1028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1164..1186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1168..1199
FT /evidence="ECO:0000255"
FT COMPBIAS 1013..1028
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1171..1186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U430"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U430"
FT MOD_RES 1199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U430"
FT VAR_SEQ 1..1494
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_023141"
FT VAR_SEQ 1..1179
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_030354"
FT VAR_SEQ 1180..1211
FT /note="EERRQKARERQQKLLAEFASRQKSFMETAMDV -> MIASKQRQFTEVFRIM
FT SSTFSQSRFLYAAVVT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_023142"
FT VAR_SEQ 1485
FT /note="N -> NFCFIISPFTKSEIILCQYRKSHDKVYPKY (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036405"
FT CONFLICT 1791
FT /note="L -> F (in Ref. 2; BAC87032)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1888 AA; 212433 MW; 5F5525B33D2E9153 CRC64;
MAAAAAAAVG GQQPSQPELP APGLALDKAA TAAHLKAALS RPDNRAGAEE LQALLERVLS
AERPLAAAAG GEDAAAAGGG GGPGAAEEEA LEWCKCLLAG GGGYDEFCAA VRAYDPAALC
GLVWTANFVA YRCRTCGISP CMSLCAECFH QGDHTGHDFN MFRSQAGGAC DCGDSNVMRE
SGFCKRHQIK SSSNIPCVPK DLLMMSEFVL PRFIFCLIQY LREGYNEPAA DGPSEKDLNK
VLQLLEPQIS FLEDLTKMGG AMRSVLTQVL TNQQNYKDLT SGLGENACVK KSHEKYLIAL
KSSGLTYPED KLVYGVQEPS AGTSSLAVQG FIGATGTLGQ VDSSDEDDQD GSQGLGKRKR
VKLSSGTKDQ SIMDVLKHKS FLEELLFWTI KYEFPQKMVT FLLNMLPDQE YKVAFTKTFV
QHYAFIMKTL KKSHESDTMS NRIVHISVQL FSNEELARQV TEECQLLDIM VTVLLYMMES
CLIKSELQDE ENSLHVVVNC GEALLKNNTY WPLVSDFINI LSHQSVAKRF LEDHGLLVTW
MNFVSFFQGM NLNKRELNEH VEFESQTYYA AFAAELEACA QPMWGLLSHC KVRETQEYTR
NVVRYCLEAL QDWFDAINFV DEPAPNQVTF HLPLHRYYAM FLSKAVKCQE LDLDSVLPDQ
EMLMKLMIHP LQIQASLAEI HSNMWVRNGL QIKGQAMTYV QSHFCNSMID PDIYLLQVCA
SRLDPDYFIS SVFERFKVVD LLTMASQHQN TVLDAEHERS MLEGALTFLV ILLSLRLHLG
MSDDEILRAE MVAQLCMNDR THSSLLDLIP ENPNPKSGII PGSYSFESVL SAVADFKAPV
FEPGGSMQQG MYTPKAEVWD QEFDPVMVIL RTVYRRDVQS AMDRYTAFLK QSGKFPGNPW
PPYKKRTSLH PSYKGLMRLL HCKTLHIVLF TLLYKILMDH QNLSEHVLCM VLYLIELGLE
NSAEEESDEE ASVGGPERCH DSWFPGSNLV SNMRHFINYV RVRVPETAPE VKRDSPASTS
SDNLGSLQNS GTAQVFSLVA ERRKKFQEII NRSSSEANQV VRPKTSSKWS APGSAPQLTT
AILEIKESIL SLLIKLHHKL SGKQNSYYPP WLDDIEILIQ PEIPKYSHGD GITAVERILL
KAASQSRMNK RIIEEICRKV TPPVPPKKVT AAEKKTLDKE ERRQKARERQ QKLLAEFASR
QKSFMETAMD VDSPENDIPM EITTAEPQVS EAVYDCVICG QSGPSSEDRP TGLVVLLQAS
SVLGQCRDNV EPKKLPISEE EQIYPWDTCA AVHDVRLSLL QRYFKDSSCL LAVSIGWEGG
VYVQTCGHTL HIDCHKSYME SLRNDQVLQG FSVDKGEFTC PLCRQFANSV LPCYPGSNVE
NNPWQRPSNK SIQDLIKEVE ELQGRPGAFP SETNLSKEME SVMKDIKNTT QKKYRDYSKT
PGSPDNDFLF MYSVARTNLE LELIHRGGNL CSGGASTAGK RSCLNQLFHV LALHMRLYSI
DSEYNPWRKL TQLEEMNPQL GYEEQQPEVP ILYHDVTSLL LIQILMMPQP LRKDHFTCIV
KVLFTLLYTQ ALAALSVKCS EEDRSAWKHA GALKKSTCDA EKSYEVLLSF VISELFKGKL
YHEEGTQECA MVNPIAWSPE SMEKCLQDFC LPFLRITSLL QHHLFGEDLP SCQEEEEFSV
LASCLGLLPT FYQTEHPFIS ASCLDWPVPA FDIITQWCFE IKSFTERHAE QGKALLIQES
KWKLPHLLQL PENYNTIFQY YHRKTCSVCT KVPKDPAVCL VCGTFVCLKG LCCKQQSYCE
CVLHSQNCGA GTGIFLLINA SVIIIIRGHR FCLWGSVYLD AHGEEDRDLR RGKPLYICKE
RYKVLEQQWI SHTFDHINKR WGPHYNGL
