RFC5_HUMAN
ID RFC5_HUMAN Reviewed; 340 AA.
AC P40937; A8MZ62; B3KSX8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Replication factor C subunit 5;
DE AltName: Full=Activator 1 36 kDa subunit;
DE Short=A1 36 kDa subunit;
DE AltName: Full=Activator 1 subunit 5;
DE AltName: Full=Replication factor C 36 kDa subunit;
DE Short=RF-C 36 kDa subunit;
DE Short=RFC36;
GN Name=RFC5;
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=8441605; DOI=10.1093/nar/21.1.1;
RA O'Donnell M., Onrust R., Dean F.B., Chen M., Hurwitz J.;
RT "Homology in accessory proteins of replicative polymerases -- E. coli to
RT humans.";
RL Nucleic Acids Res. 21:1-3(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-13.
RG NIEHS SNPs program;
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Amygdala;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle, and Skin;
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 [6]
RP FUNCTION, AND INTERACTION WITH PCNA.
RX PubMed=8999859; DOI=10.1074/jbc.272.3.1769;
RA Mossi R., Jonsson Z.O., Allen B.L., Hardin S.H., Huebscher U.;
RT "Replication factor C interacts with the C-terminal side of proliferating
RT cell nuclear antigen.";
RL J. Biol. Chem. 272:1769-1776(1997).
RN [7]
RP INTERACTION WITH RAD17.
RX PubMed=11572977; DOI=10.1073/pnas.201373498;
RA Lindsey-Boltz L.A., Bermudez V.P., Hurwitz J., Sancar A.;
RT "Purification and characterization of human DNA damage checkpoint Rad
RT complexes.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:11236-11241(2001).
RN [8]
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: The elongation of primed DNA templates by DNA polymerase
CC delta and epsilon requires the action of the accessory proteins
CC proliferating cell nuclear antigen (PCNA) and activator 1.
CC {ECO:0000269|PubMed:8999859}.
CC -!- SUBUNIT: Heterotetramer of subunits RFC2, RFC3, RFC4 and RFC5 that can
CC form a complex either with RFC1 or with RAD17. The former interacts
CC with PCNA in the presence of ATP, while the latter has ATPase activity
CC but is not stimulated by PCNA. {ECO:0000269|PubMed:11572977,
CC ECO:0000269|PubMed:8999859}.
CC -!- INTERACTION:
CC P40937; Q03989: ARID5A; NbExp=3; IntAct=EBI-712376, EBI-948603;
CC P40937; Q13490: BIRC2; NbExp=3; IntAct=EBI-712376, EBI-514538;
CC P40937; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-712376, EBI-2548012;
CC P40937; P24863: CCNC; NbExp=5; IntAct=EBI-712376, EBI-395261;
CC P40937; Q96D03: DDIT4L; NbExp=5; IntAct=EBI-712376, EBI-742054;
CC P40937; A0A0C4DGQ7: EML2; NbExp=3; IntAct=EBI-712376, EBI-12112376;
CC P40937; Q96B26: EXOSC8; NbExp=3; IntAct=EBI-712376, EBI-371922;
CC P40937; A8MTA8-2: FAM166B; NbExp=3; IntAct=EBI-712376, EBI-12160437;
CC P40937; O76011: KRT34; NbExp=3; IntAct=EBI-712376, EBI-1047093;
CC P40937; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-712376, EBI-11742507;
CC P40937; Q9HAF1: MEAF6; NbExp=3; IntAct=EBI-712376, EBI-399266;
CC P40937; O15049: N4BP3; NbExp=5; IntAct=EBI-712376, EBI-2512055;
CC P40937; Q15742: NAB2; NbExp=8; IntAct=EBI-712376, EBI-8641936;
CC P40937; Q13285: NR5A1; NbExp=3; IntAct=EBI-712376, EBI-874629;
CC P40937; Q96T49: PPP1R16B; NbExp=3; IntAct=EBI-712376, EBI-10293968;
CC P40937; P35249: RFC4; NbExp=22; IntAct=EBI-712376, EBI-476655;
CC P40937; Q5VWN6: TASOR2; NbExp=3; IntAct=EBI-712376, EBI-745958;
CC P40937; O00635: TRIM38; NbExp=8; IntAct=EBI-712376, EBI-2130415;
CC P40937; Q99598: TSNAX; NbExp=3; IntAct=EBI-712376, EBI-742638;
CC P40937; Q6GPH4: XAF1; NbExp=3; IntAct=EBI-712376, EBI-2815120;
CC P40937; P98170: XIAP; NbExp=9; IntAct=EBI-712376, EBI-517127;
CC P40937; P17023: ZNF19; NbExp=5; IntAct=EBI-712376, EBI-12884200;
CC P40937; Q9BUY5: ZNF426; NbExp=3; IntAct=EBI-712376, EBI-743265;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P40937-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P40937-2; Sequence=VSP_043067;
CC -!- SIMILARITY: Belongs to the activator 1 small subunits family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/rfc5/";
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DR EMBL; L07540; AAB09784.1; -; mRNA.
DR EMBL; AY254323; AAO63493.1; -; Genomic_DNA.
DR EMBL; AK094575; BAG52890.1; -; mRNA.
DR EMBL; AC131159; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001866; AAH01866.1; -; mRNA.
DR EMBL; BC013961; AAH13961.1; -; mRNA.
DR CCDS; CCDS41843.2; -. [P40937-2]
DR CCDS; CCDS9185.1; -. [P40937-1]
DR RefSeq; NP_001123584.1; NM_001130112.3.
DR RefSeq; NP_001123585.1; NM_001130113.2. [P40937-2]
DR RefSeq; NP_031396.1; NM_007370.6. [P40937-1]
DR RefSeq; NP_853556.2; NM_181578.4. [P40937-2]
DR RefSeq; XP_011536945.1; XM_011538643.2. [P40937-1]
DR RefSeq; XP_011536947.1; XM_011538645.2. [P40937-1]
DR PDB; 6VVO; EM; 3.40 A; C=1-340.
DR PDBsum; 6VVO; -.
DR AlphaFoldDB; P40937; -.
DR SMR; P40937; -.
DR BioGRID; 111917; 178.
DR ComplexPortal; CPX-415; DNA replication factor C complex.
DR CORUM; P40937; -.
DR DIP; DIP-36433N; -.
DR IntAct; P40937; 85.
DR MINT; P40937; -.
DR STRING; 9606.ENSP00000408295; -.
DR ChEMBL; CHEMBL4296000; -.
DR GlyGen; P40937; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P40937; -.
DR MetOSite; P40937; -.
DR PhosphoSitePlus; P40937; -.
DR BioMuta; RFC5; -.
DR DMDM; 728777; -.
DR EPD; P40937; -.
DR jPOST; P40937; -.
DR MassIVE; P40937; -.
DR MaxQB; P40937; -.
DR PaxDb; P40937; -.
DR PeptideAtlas; P40937; -.
DR PRIDE; P40937; -.
DR ProteomicsDB; 55389; -. [P40937-1]
DR ProteomicsDB; 55390; -. [P40937-2]
DR Antibodypedia; 18857; 126 antibodies from 30 providers.
DR DNASU; 5985; -.
DR Ensembl; ENST00000392542.6; ENSP00000376325.2; ENSG00000111445.14. [P40937-2]
DR Ensembl; ENST00000454402.7; ENSP00000408295.2; ENSG00000111445.14. [P40937-1]
DR GeneID; 5985; -.
DR KEGG; hsa:5985; -.
DR MANE-Select; ENST00000454402.7; ENSP00000408295.2; NM_007370.7; NP_031396.1.
DR UCSC; uc001twq.4; human. [P40937-1]
DR CTD; 5985; -.
DR DisGeNET; 5985; -.
DR GeneCards; RFC5; -.
DR HGNC; HGNC:9973; RFC5.
DR HPA; ENSG00000111445; Low tissue specificity.
DR MIM; 600407; gene.
DR neXtProt; NX_P40937; -.
DR OpenTargets; ENSG00000111445; -.
DR PharmGKB; PA34342; -.
DR VEuPathDB; HostDB:ENSG00000111445; -.
DR eggNOG; KOG0990; Eukaryota.
DR GeneTree; ENSGT00550000075072; -.
DR HOGENOM; CLU_042324_2_0_1; -.
DR InParanoid; P40937; -.
DR OMA; TRTIFCG; -.
DR OrthoDB; 1071197at2759; -.
DR PhylomeDB; P40937; -.
DR TreeFam; TF300810; -.
DR BRENDA; 3.6.4.B8; 2681.
DR PathwayCommons; P40937; -.
DR Reactome; R-HSA-110312; Translesion synthesis by REV1.
DR Reactome; R-HSA-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-HSA-110320; Translesion Synthesis by POLH.
DR Reactome; R-HSA-174411; Polymerase switching on the C-strand of the telomere.
DR Reactome; R-HSA-176187; Activation of ATR in response to replication stress.
DR Reactome; R-HSA-5651801; PCNA-Dependent Long Patch Base Excision Repair.
DR Reactome; R-HSA-5655862; Translesion synthesis by POLK.
DR Reactome; R-HSA-5656121; Translesion synthesis by POLI.
DR Reactome; R-HSA-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-HSA-5685938; HDR through Single Strand Annealing (SSA).
DR Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-HSA-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
DR Reactome; R-HSA-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR Reactome; R-HSA-5696400; Dual Incision in GG-NER.
DR Reactome; R-HSA-6782135; Dual incision in TC-NER.
DR Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-HSA-69091; Polymerase switching.
DR Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
DR Reactome; R-HSA-9709570; Impaired BRCA2 binding to RAD51.
DR SignaLink; P40937; -.
DR SIGNOR; P40937; -.
DR BioGRID-ORCS; 5985; 779 hits in 1085 CRISPR screens.
DR ChiTaRS; RFC5; human.
DR GeneWiki; RFC5; -.
DR GenomeRNAi; 5985; -.
DR Pharos; P40937; Tbio.
DR PRO; PR:P40937; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P40937; protein.
DR Bgee; ENSG00000111445; Expressed in pons and 218 other tissues.
DR ExpressionAtlas; P40937; baseline and differential.
DR Genevisible; P40937; HS.
DR GO; GO:0031390; C:Ctf18 RFC-like complex; IDA:UniProtKB.
DR GO; GO:0005663; C:DNA replication factor C complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0019899; F:enzyme binding; NAS:UniProtKB.
DR GO; GO:0032508; P:DNA duplex unwinding; IEA:GOC.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; NAS:UniProtKB.
DR GO; GO:0006261; P:DNA-templated DNA replication; IBA:GO_Central.
DR GO; GO:1900264; P:positive regulation of DNA-directed DNA polymerase activity; IDA:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013748; Rep_factorC_C.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF08542; Rep_fac_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF48019; SSF48019; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW DNA replication; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..340
FT /note="Replication factor C subunit 5"
FT /id="PRO_0000121751"
FT BINDING 60..67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT VAR_SEQ 1..22
FT /note="METSALKQQEQPAATKIRNLPW -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043067"
FT VARIANT 13
FT /note="A -> T (in dbSNP:rs5745796)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_018749"
FT HELIX 22..25
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 38..49
FT /evidence="ECO:0007829|PDB:6VVO"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 66..77
FT /evidence="ECO:0007829|PDB:6VVO"
FT TURN 82..85
FT /evidence="ECO:0007829|PDB:6VVO"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 104..109
FT /evidence="ECO:0007829|PDB:6VVO"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:6VVO"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 132..144
FT /evidence="ECO:0007829|PDB:6VVO"
FT STRAND 147..156
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 163..168
FT /evidence="ECO:0007829|PDB:6VVO"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 179..192
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 201..209
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 213..226
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 234..238
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 244..255
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 259..272
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 277..290
FT /evidence="ECO:0007829|PDB:6VVO"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 298..312
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 318..329
FT /evidence="ECO:0007829|PDB:6VVO"
SQ SEQUENCE 340 AA; 38497 MW; E31E7B8C79933BCE CRC64;
METSALKQQE QPAATKIRNL PWVEKYRPQT LNDLISHQDI LSTIQKFINE DRLPHLLLYG
PPGTGKTSTI LACAKQLYKD KEFGSMVLEL NASDDRGIDI IRGPILSFAS TRTIFKKGFK
LVILDEADAM TQDAQNALRR VIEKFTENTR FCLICNYLSK IIPALQSRCT RFRFGPLTPE
LMVPRLEHVV EEEKVDISED GMKALVTLSS GDMRRALNIL QSTNMAFGKV TEETVYTCTG
HPLKSDIANI LDWMLNQDFT TAYRNITELK TLKGLALHDI LTEIHLFVHR VDFPSSVRIH
LLTKMADIEY RLSVGTNEKI QLSSLIAAFQ VTRDLIVAEA
