OBI1_HUMAN
ID OBI1_HUMAN Reviewed; 726 AA.
AC Q5W0B1; B2RN99; Q8TBY2; Q9H0T2; Q9H8M0;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=ORC ubiquitin ligase 1 {ECO:0000305};
DE Short=OBI1 {ECO:0000303|PubMed:31160578};
DE EC=2.3.2.27 {ECO:0000269|PubMed:31160578};
DE AltName: Full=RING finger protein 219;
GN Name=OBI1 {ECO:0000312|HGNC:HGNC:20308}; Synonyms=C13orf7, RNF219;
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].
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Testis;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 175-726.
RC TISSUE=Placenta;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-719, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210; SER-526; SER-561 AND
RP SER-721, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, CHROMATIN-BINDING, INTERACTION WITH ORC
RP COMPLEX, MUTAGENESIS OF CYS-38, SUBCELLULAR LOCATION, AND
RP AUTO-UBIQUITINATION.
RX PubMed=31160578; DOI=10.1038/s41467-019-10321-x;
RA Coulombe P., Nassar J., Peiffer I., Stanojcic S., Sterkers Y.,
RA Delamarre A., Bocquet S., Mechali M.;
RT "The ORC ubiquitin ligase OBI1 promotes DNA replication origin firing.";
RL Nat. Commun. 10:2426-2426(2019).
CC -!- FUNCTION: E3 ubiquitin ligase essential for DNA replication origin
CC activation during S phase (PubMed:31160578). Acts as a replication
CC origin selector which selects the origins to be fired and catalyzes the
CC multi-mono-ubiquitination of a subset of chromatin-bound ORC3 and ORC5
CC during S-phase (PubMed:31160578). {ECO:0000269|PubMed:31160578}.
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; Evidence={ECO:0000269|PubMed:31160578};
CC -!- SUBUNIT: Associates with ORC complex (PubMed:31160578). Binds to
CC chromatin; association is cell cycle-regulated, absent from mitotic
CC chromosomes, is associated with chromatin from G1 and partially
CC released from chromatin from mid S-phase (PubMed:31160578).
CC {ECO:0000269|PubMed:31160578}.
CC -!- INTERACTION:
CC Q5W0B1; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-2562035, EBI-5235340;
CC Q5W0B1; Q8N8B7: TCEANC; NbExp=3; IntAct=EBI-2562035, EBI-954696;
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:31160578}.
CC Note=Association to chromatin is cell cycle-regulated, absent from
CC mitotic chromosomes, is associated with chromatin from G1 and partially
CC released from chromatin from mid S-phase.
CC {ECO:0000269|PubMed:31160578}.
CC -!- PTM: Auto-ubiquitinated. {ECO:0000269|PubMed:31160578}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14594.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BC028586; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAB66586.3; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AL136651; CAB66586.3; ALT_SEQ; mRNA.
DR EMBL; AL139319; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028586; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CH471093; EAW80586.1; -; Genomic_DNA.
DR EMBL; BC136764; AAI36765.1; -; mRNA.
DR EMBL; BC136765; AAI36766.1; -; mRNA.
DR EMBL; AK023511; BAB14594.1; ALT_INIT; mRNA.
DR CCDS; CCDS31997.1; -.
DR RefSeq; NP_078822.3; NM_024546.3.
DR AlphaFoldDB; Q5W0B1; -.
DR SMR; Q5W0B1; -.
DR BioGRID; 122736; 132.
DR IntAct; Q5W0B1; 46.
DR MINT; Q5W0B1; -.
DR STRING; 9606.ENSP00000282003; -.
DR iPTMnet; Q5W0B1; -.
DR PhosphoSitePlus; Q5W0B1; -.
DR BioMuta; RNF219; -.
DR DMDM; 73917812; -.
DR EPD; Q5W0B1; -.
DR jPOST; Q5W0B1; -.
DR MassIVE; Q5W0B1; -.
DR MaxQB; Q5W0B1; -.
DR PaxDb; Q5W0B1; -.
DR PeptideAtlas; Q5W0B1; -.
DR PRIDE; Q5W0B1; -.
DR ProteomicsDB; 65758; -.
DR Antibodypedia; 24695; 162 antibodies from 23 providers.
DR DNASU; 79596; -.
DR Ensembl; ENST00000282003.7; ENSP00000282003.6; ENSG00000152193.8.
DR GeneID; 79596; -.
DR KEGG; hsa:79596; -.
DR MANE-Select; ENST00000282003.7; ENSP00000282003.6; NM_024546.4; NP_078822.3.
DR UCSC; uc001vkw.2; human.
DR CTD; 79596; -.
DR DisGeNET; 79596; -.
DR GeneCards; OBI1; -.
DR HGNC; HGNC:20308; OBI1.
DR HPA; ENSG00000152193; Low tissue specificity.
DR MIM; 615906; gene.
DR neXtProt; NX_Q5W0B1; -.
DR OpenTargets; ENSG00000152193; -.
DR VEuPathDB; HostDB:ENSG00000152193; -.
DR eggNOG; ENOG502QTFT; Eukaryota.
DR GeneTree; ENSGT00390000013512; -.
DR HOGENOM; CLU_023039_0_0_1; -.
DR InParanoid; Q5W0B1; -.
DR OMA; PTNFAEN; -.
DR OrthoDB; 487392at2759; -.
DR PhylomeDB; Q5W0B1; -.
DR TreeFam; TF329331; -.
DR PathwayCommons; Q5W0B1; -.
DR SignaLink; Q5W0B1; -.
DR BioGRID-ORCS; 79596; 13 hits in 1114 CRISPR screens.
DR ChiTaRS; RNF219; human.
DR GenomeRNAi; 79596; -.
DR Pharos; Q5W0B1; Tdark.
DR PRO; PR:Q5W0B1; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q5W0B1; protein.
DR Bgee; ENSG00000152193; Expressed in secondary oocyte and 194 other tissues.
DR Genevisible; Q5W0B1; HS.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
DR GO; GO:0006513; P:protein monoubiquitination; IDA:UniProtKB.
DR GO; GO:0006275; P:regulation of DNA replication; IDA:UniProtKB.
DR CDD; cd16562; RING-HC_RNF219; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR039209; OBI1.
DR InterPro; IPR035691; RNF219_RING-HC.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR14609; PTHR14609; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Chromosome; Coiled coil; Metal-binding; Phosphoprotein; Reference proteome;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..726
FT /note="ORC ubiquitin ligase 1"
FT /id="PRO_0000055876"
FT ZN_FING 18..56
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 276..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 87..129
FT /evidence="ECO:0000255"
FT COILED 155..270
FT /evidence="ECO:0000255"
FT COMPBIAS 295..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 526
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 553
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K2Y0"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 568
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K2Y0"
FT MOD_RES 570
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K2Y0"
FT MOD_RES 719
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 721
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MUTAGEN 38
FT /note="C->S: Loss of E3 ubiquitin transferase activity. No
FT effect on association with ORC complex."
FT /evidence="ECO:0000269|PubMed:31160578"
FT CONFLICT 126
FT /note="T -> A (in Ref. 1; CAB66586)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="L -> F (in Ref. 1; CAB66586)"
FT /evidence="ECO:0000305"
FT CONFLICT 462
FT /note="P -> T (in Ref. 1; CAB66586)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 726 AA; 81116 MW; 2ADD8EAE5282A1CF CRC64;
MAQTVQNVTL SLTLPITCHI CLGKVRQPVI CINNHVFCSI CIDLWLKNNS QCPACRVPIT
PENPCKEIIG GTSESEPMLS HTVRKHLRKT RLELLHKEYE DEIDCLQKEV EELKSKNLSL
ESQIKTILDP LTLVQGNQNE DKHLVTDNPS KINPETVAEW KKKLRTANEI YEKVKDDVDK
LKEANKKLKL ENGGLVRENL RLKAEVDNRS PQKFGRFAVA ALQSKVEQYE RETNRLKKAL
ERSDKYIEEL ESQVAQLKNS SEEKEAMNSI CQTALSADGK GSKGSEEDVV SKNQGDSARK
QPGSSTSSSS HLAKPSSSRL CDTSSARQES TSKADLNCSK NKDLYQEQVE VMLDVTDTSM
DTYLEREWGN KPSDCVPYKD EELYDLPAPC TPLSLSCLQL STPENRESSV VQAGGSKKHS
NHLRKLVFDD FCDSSNVSNK DSSEDDISRS ENEKKSECFS SPKTGFWDCC STSYAQNLDF
ESSEGNTIAN SVGEISSKLS EKSGLCLSKR LNSIRSFEMN RTRTSSEASM DAAYLDKISE
LDSMMSESDN SKSPCNNGFK SLDLDGLSKS SQGSEFLEEP DKLEEKTELN LSKGSLTNDQ
LENGSEWKPT SFFLLSPSDQ EMNEDFSLHS SSCPVTNEIK PPSCLFQTEF SQGILLSSSH
RLFEDQRFGS SLFKMSSEMH SLHNHLQSPW STSFVPEKRN KNVNQSTKRK IQSSLSSASP
SKATKS
