ORC5_HUMAN
ID ORC5_HUMAN Reviewed; 435 AA.
AC O43913; A4D0P8; O60590; O95268;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Origin recognition complex subunit 5;
GN Name=ORC5; Synonyms=ORC5L;
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 [MRNA] (ISOFORM 1).
RX PubMed=9829972; DOI=10.1074/jbc.273.49.32421;
RA Tugal T., Zou-Yang X.H., Gavin K., Pappin D., Canas B., Kobayashi R.,
RA Hunt T., Stillman B.;
RT "The Orc4p and Orc5p subunits of the Xenopus and human origin recognition
RT complex are related to Orc1p and Cdc6p.";
RL J. Biol. Chem. 273:32421-32429(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9417919; DOI=10.1006/geno.1997.5003;
RA Ishiai M., Dean F.B., Okumura K., Abe M., Moon K.-Y., Amin A.A.,
RA Kagotani K., Taguchi H., Murakami Y., Hanaoka F., O'Donnell M., Hurwitz J.,
RA Eki T.;
RT "Isolation of human and fission yeast homologues of the budding yeast
RT origin recognition complex subunit ORC5: human homologue (ORC5L) maps to
RT 7q22.";
RL Genomics 46:294-298(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING, TISSUE
RP SPECIFICITY, AND VARIANT ARG-37.
RX PubMed=9765232; DOI=10.1074/jbc.273.42.27137;
RA Quintana D.G., Thome K.C., Hou Z.-H., Ligon A.H., Morton C.C., Dutta A.;
RT "ORC5L, a new member of the human origin recognition complex, is deleted in
RT uterine leiomyomas and malignant myeloid diseases.";
RL J. Biol. Chem. 273:27137-27145(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
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 [8]
RP IDENTIFICATION IN THE ORC COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP ASSEMBLY OF THE ORC COMPLEX.
RX PubMed=12909626; DOI=10.1074/jbc.m307535200;
RA Ohta S., Tatsumi Y., Fujita M., Tsurimoto T., Obuse C.;
RT "The ORC1 cycle in human cells: II. Dynamic changes in the human ORC
RT complex during the cell cycle.";
RL J. Biol. Chem. 278:41535-41540(2003).
RN [9]
RP RECONSTITUTION OF THE ORC COMPLEX, AND DISASSEMBLY OF THE ORC COMPLEX.
RX PubMed=17716973; DOI=10.1074/jbc.m705905200;
RA Siddiqui K., Stillman B.;
RT "ATP-dependent assembly of the human origin recognition complex.";
RL J. Biol. Chem. 282:32370-32383(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP FUNCTION, UBIQUITINATION, AND SUBCELLULAR LOCATION.
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: Component of the origin recognition complex (ORC) that binds
CC origins of replication. DNA-binding is ATP-dependent. The specific DNA
CC sequences that define origins of replication have not been identified
CC yet. ORC is required to assemble the pre-replication complex necessary
CC to initiate DNA replication. {ECO:0000269|PubMed:31160578}.
CC -!- SUBUNIT: Component of ORC, a complex composed of at least 6 subunits:
CC ORC1, ORC2, ORC3, ORC4, ORC5 and ORC6. ORC is regulated in a cell-cycle
CC dependent manner. It is sequentially assembled at the exit from
CC anaphase of mitosis and disassembled as cells enter S phase.
CC {ECO:0000269|PubMed:12909626}.
CC -!- INTERACTION:
CC O43913; Q13415: ORC1; NbExp=11; IntAct=EBI-374928, EBI-374847;
CC O43913; Q13416: ORC2; NbExp=15; IntAct=EBI-374928, EBI-374957;
CC O43913; Q9UBD5: ORC3; NbExp=15; IntAct=EBI-374928, EBI-374916;
CC O43913; O43929: ORC4; NbExp=2; IntAct=EBI-374928, EBI-374889;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31160578}. Chromosome
CC {ECO:0000269|PubMed:31160578}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O43913-1; Sequence=Displayed;
CC Name=2; Synonyms=ORC5T;
CC IsoId=O43913-2; Sequence=VSP_042037;
CC -!- TISSUE SPECIFICITY: Abundant in spleen, ovary, prostate, testis, and
CC colon mucosa. {ECO:0000269|PubMed:9765232}.
CC -!- PTM: Multi-mono-ubiquitinated by OBI1; ubiquitination is important for
CC efficient DNA replication origin site activation. Ubiquitination levels
CC are low in mitotic and early G1-phAse cells and are induced in late
CC G1-/early S-phase, peaking in S-phase and decrease toward the end of
CC the cell cycle. {ECO:0000269|PubMed:31160578}.
CC -!- MISCELLANEOUS: [Isoform 2]: Does not interact with ORC2. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ORC5 family. {ECO:0000305}.
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DR EMBL; AF047599; AAC80283.1; -; mRNA.
DR EMBL; U92538; AAC51933.1; -; mRNA.
DR EMBL; AF049127; AAC63972.1; -; mRNA.
DR EMBL; AF081459; AAC64401.1; -; mRNA.
DR EMBL; AC002067; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC007393; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236947; EAL24409.1; -; Genomic_DNA.
DR EMBL; CH471070; EAW83341.1; -; Genomic_DNA.
DR EMBL; BC023652; AAH23652.1; -; mRNA.
DR CCDS; CCDS47681.1; -. [O43913-2]
DR CCDS; CCDS5734.1; -. [O43913-1]
DR RefSeq; NP_002544.1; NM_002553.3. [O43913-1]
DR RefSeq; NP_859531.1; NM_181747.3. [O43913-2]
DR PDB; 5UJ7; X-ray; 3.39 A; E/F=1-284.
DR PDB; 5UJM; EM; 18.00 A; E=1-435.
DR PDB; 7CTE; EM; 3.80 A; E=1-435.
DR PDB; 7CTF; EM; 4.80 A; E=1-435.
DR PDB; 7CTG; EM; 5.00 A; E=1-435.
DR PDB; 7JPO; EM; 3.20 A; E=1-435.
DR PDB; 7JPP; EM; 3.70 A; E=1-435.
DR PDB; 7JPQ; EM; 3.50 A; E=1-435.
DR PDB; 7JPR; EM; 4.00 A; E=1-435.
DR PDB; 7JPS; EM; 4.40 A; E=1-435.
DR PDBsum; 5UJ7; -.
DR PDBsum; 5UJM; -.
DR PDBsum; 7CTE; -.
DR PDBsum; 7CTF; -.
DR PDBsum; 7CTG; -.
DR PDBsum; 7JPO; -.
DR PDBsum; 7JPP; -.
DR PDBsum; 7JPQ; -.
DR PDBsum; 7JPR; -.
DR PDBsum; 7JPS; -.
DR AlphaFoldDB; O43913; -.
DR SMR; O43913; -.
DR BioGRID; 111043; 82.
DR ComplexPortal; CPX-1880; Nuclear origin of replication recognition complex.
DR CORUM; O43913; -.
DR DIP; DIP-29691N; -.
DR IntAct; O43913; 40.
DR MINT; O43913; -.
DR STRING; 9606.ENSP00000297431; -.
DR GlyGen; O43913; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O43913; -.
DR PhosphoSitePlus; O43913; -.
DR SwissPalm; O43913; -.
DR BioMuta; ORC5; -.
DR EPD; O43913; -.
DR jPOST; O43913; -.
DR MassIVE; O43913; -.
DR MaxQB; O43913; -.
DR PaxDb; O43913; -.
DR PeptideAtlas; O43913; -.
DR PRIDE; O43913; -.
DR ProteomicsDB; 49227; -. [O43913-1]
DR ProteomicsDB; 49228; -. [O43913-2]
DR Antibodypedia; 31233; 97 antibodies from 23 providers.
DR DNASU; 5001; -.
DR Ensembl; ENST00000297431.9; ENSP00000297431.4; ENSG00000164815.11. [O43913-1]
DR Ensembl; ENST00000447452.6; ENSP00000395747.2; ENSG00000164815.11. [O43913-2]
DR GeneID; 5001; -.
DR KEGG; hsa:5001; -.
DR MANE-Select; ENST00000297431.9; ENSP00000297431.4; NM_002553.4; NP_002544.1.
DR UCSC; uc003vcb.3; human. [O43913-1]
DR CTD; 5001; -.
DR DisGeNET; 5001; -.
DR GeneCards; ORC5; -.
DR HGNC; HGNC:8491; ORC5.
DR HPA; ENSG00000164815; Low tissue specificity.
DR MIM; 602331; gene.
DR neXtProt; NX_O43913; -.
DR OpenTargets; ENSG00000164815; -.
DR PharmGKB; PA32812; -.
DR VEuPathDB; HostDB:ENSG00000164815; -.
DR eggNOG; KOG2543; Eukaryota.
DR GeneTree; ENSGT00390000009380; -.
DR HOGENOM; CLU_028223_0_0_1; -.
DR InParanoid; O43913; -.
DR OMA; QLRRWHG; -.
DR PhylomeDB; O43913; -.
DR TreeFam; TF101095; -.
DR BRENDA; 3.6.4.B8; 2681.
DR PathwayCommons; O43913; -.
DR Reactome; R-HSA-113507; E2F-enabled inhibition of pre-replication complex formation.
DR Reactome; R-HSA-176187; Activation of ATR in response to replication stress.
DR Reactome; R-HSA-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-HSA-68689; CDC6 association with the ORC:origin complex.
DR Reactome; R-HSA-68867; Assembly of the pre-replicative complex.
DR Reactome; R-HSA-68949; Orc1 removal from chromatin.
DR Reactome; R-HSA-68962; Activation of the pre-replicative complex.
DR SignaLink; O43913; -.
DR SIGNOR; O43913; -.
DR BioGRID-ORCS; 5001; 448 hits in 1103 CRISPR screens.
DR ChiTaRS; ORC5; human.
DR GeneWiki; ORC5; -.
DR GeneWiki; ORC5L; -.
DR GenomeRNAi; 5001; -.
DR Pharos; O43913; Tbio.
DR PRO; PR:O43913; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; O43913; protein.
DR Bgee; ENSG00000164815; Expressed in secondary oocyte and 194 other tissues.
DR ExpressionAtlas; O43913; baseline and differential.
DR Genevisible; O43913; HS.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0000781; C:chromosome, telomeric region; HDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005664; C:nuclear origin of replication recognition complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0000808; C:origin recognition complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003688; F:DNA replication origin binding; IBA:GO_Central.
DR GO; GO:0000166; F:nucleotide binding; TAS:ProtInc.
DR GO; GO:0006260; P:DNA replication; NAS:UniProtKB.
DR GO; GO:0006270; P:DNA replication initiation; IBA:GO_Central.
DR GO; GO:0006275; P:regulation of DNA replication; IDA:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR041664; AAA_16.
DR InterPro; IPR020796; ORC5.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR12705; PTHR12705; 1.
DR Pfam; PF13191; AAA_16; 1.
DR Pfam; PF14630; ORC5_C; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Chromosome;
KW DNA replication; Nucleotide-binding; Nucleus; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..435
FT /note="Origin recognition complex subunit 5"
FT /id="PRO_0000127092"
FT BINDING 37..44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VAR_SEQ 294..435
FT /note="LSAHTHVELPYYSKFILIAAYLASYNPARTDKRFFLKHHGKIKKTNFLKKHE
FT KTSNHLLGPKPFPLDRLLAILYSIVDSRVAPTANIFSQITSLVTLQLLTLVGHDDQLDG
FT PKYKCTVSLDFIRAIARTVNFDIIKYLYDFL -> IRGSIETVTGDTSSANYQDTKVNT
FT KEHSVRK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9765232"
FT /id="VSP_042037"
FT VARIANT 37
FT /note="G -> R (in dbSNP:rs1056677)"
FT /evidence="ECO:0000269|PubMed:9765232"
FT /id="VAR_011800"
FT VARIANT 52
FT /note="K -> N (in dbSNP:rs2307413)"
FT /id="VAR_014524"
FT VARIANT 166
FT /note="R -> C (in dbSNP:rs2307402)"
FT /id="VAR_014525"
FT HELIX 13..22
FT /evidence="ECO:0007829|PDB:7JPO"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:7JPO"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:7JPO"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 43..53
FT /evidence="ECO:0007829|PDB:7JPO"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:7JPO"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 69..84
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 99..110
FT /evidence="ECO:0007829|PDB:7JPO"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:7JPO"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:7JPO"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 137..142
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 144..148
FT /evidence="ECO:0007829|PDB:7JPO"
FT STRAND 152..160
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:7JPO"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 184..191
FT /evidence="ECO:0007829|PDB:7JPO"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:5UJ7"
FT HELIX 201..215
FT /evidence="ECO:0007829|PDB:7JPO"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 222..236
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 238..242
FT /evidence="ECO:0007829|PDB:7JPO"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 250..267
FT /evidence="ECO:0007829|PDB:7JPO"
FT TURN 268..271
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 275..283
FT /evidence="ECO:0007829|PDB:7JPO"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 304..317
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 324..327
FT /evidence="ECO:0007829|PDB:7JPO"
FT TURN 350..352
FT /evidence="ECO:0007829|PDB:7JPQ"
FT HELIX 359..369
FT /evidence="ECO:0007829|PDB:7JPO"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 378..389
FT /evidence="ECO:0007829|PDB:7JPO"
FT STRAND 392..395
FT /evidence="ECO:0007829|PDB:7JPO"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:7JPO"
FT STRAND 407..409
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 413..422
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 428..431
FT /evidence="ECO:0007829|PDB:7JPO"
SQ SEQUENCE 435 AA; 50283 MW; 0FEB0E829C124745 CRC64;
MPHLENVVLC RESQVSILQS LFGERHHFSF PSIFIYGHTA SGKTYVTQTL LKTLELPHVF
VNCVECFTLR LLLEQILNKL NHLSSSEDGC STEITCETFN DFVRLFKQVT TAENLKDQTV
YIVLDKAEYL RDMEANLLPG FLRLQELADR NVTVLFLSEI VWEKFRPNTG CFEPFVLYFP
DYSIGNLQKI LSHDHPPEYS ADFYAAYINI LLGVFYTVCR DLKELRHLAV LNFPKYCEPV
VKGEASERDT RKLWRNIEPH LKKAMQTVYL REISSSQWEK LQKDDTDPGQ LKGLSAHTHV
ELPYYSKFIL IAAYLASYNP ARTDKRFFLK HHGKIKKTNF LKKHEKTSNH LLGPKPFPLD
RLLAILYSIV DSRVAPTANI FSQITSLVTL QLLTLVGHDD QLDGPKYKCT VSLDFIRAIA
RTVNFDIIKY LYDFL
