RPC9_HUMAN
ID RPC9_HUMAN Reviewed; 148 AA.
AC O75575; A8MUZ4; A8MW23; B2R4H4; B4E198; Q3KRA3; Q5HYF1; Q8IXL4;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=DNA-directed RNA polymerase III subunit RPC9;
DE Short=RNA polymerase III subunit C9;
DE AltName: Full=Calcitonin gene-related peptide-receptor component protein;
DE Short=CGRP-RCP;
DE Short=CGRP-receptor component protein;
DE Short=CGRPRCP;
DE Short=HsC17;
GN Name=CRCP;
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).
RA Luebke A.E., Dahl G.P., Dickerson I.M.;
RT "Human CGRP-receptor component protein (RCP) ORF.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=10067875; DOI=10.1210/endo.140.3.6541;
RA Balkan W., Oates E.L., Howard G.A., Roos B.A.;
RT "Testes exhibit elevated expression of calcitonin gene-related peptide
RT receptor component protein.";
RL Endocrinology 140:1459-1469(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Adrenal gland, Brain, and Kidney;
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 MRNA] (ISOFORM 4).
RC TISSUE=Fetal muscle;
RX PubMed=16344560; DOI=10.1101/gr.4039406;
RA Kimura K., Wakamatsu A., Suzuki Y., Ota T., Nishikawa T., Yamashita R.,
RA Yamamoto J., Sekine M., Tsuritani K., Wakaguri H., Ishii S., Sugiyama T.,
RA Saito K., Isono Y., Irie R., Kushida N., Yoneyama T., Otsuka R., Kanda K.,
RA Yokoi T., Kondo H., Wagatsuma M., Murakawa K., Ishida S., Ishibashi T.,
RA Takahashi-Fujii A., Tanase T., Nagai K., Kikuchi H., Nakai K., Isogai T.,
RA Sugano S.;
RT "Diversification of transcriptional modulation: large-scale identification
RT and characterization of putative alternative promoters of human genes.";
RL Genome Res. 16:55-65(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Adipose tissue;
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 [6]
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 [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=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 [9]
RP IDENTIFICATION IN THE RNA POL III COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND INTERACTION WITH RPC8.
RX PubMed=12391170; DOI=10.1128/mcb.22.22.8044-8055.2002;
RA Hu P., Wu S., Sun Y., Yuan C.-C., Kobayashi R., Myers M.P., Hernandez N.;
RT "Characterization of human RNA polymerase III identifies orthologues for
RT Saccharomyces cerevisiae RNA polymerase III subunits.";
RL Mol. Cell. Biol. 22:8044-8055(2002).
RN [10]
RP IDENTIFICATION IN THE RNA POL III COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=12482973; DOI=10.1128/mcb.23.1.195-205.2003;
RA Siaut M., Zaros C., Levivier E., Ferri M.L., Court M., Werner M.,
RA Callebaut I., Thuriaux P., Sentenac A., Conesa C.;
RT "An Rpb4/Rpb7-like complex in yeast RNA polymerase III contains the
RT orthologue of mammalian CGRP-RCP.";
RL Mol. Cell. Biol. 23:195-205(2003).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Specific peripheric component of RNA polymerase III which synthesizes
CC small RNAs, such as 5S rRNA and tRNAs. Plays a key role in sensing and
CC limiting infection by intracellular bacteria and DNA viruses. Acts as
CC nuclear and cytosolic DNA sensor involved in innate immune response.
CC Can sense non-self dsDNA that serves as template for transcription into
CC dsRNA. The non-self RNA polymerase III transcripts induce type I
CC interferon and NF- Kappa-B through the RIG-I pathway (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: Accessory protein for the calcitonin gene-related peptide
CC (CGRP) receptor. It modulates CGRP responsiveness in a variety of
CC tissues.
CC -!- SUBUNIT: Component of the RNA polymerase III (Pol III) complex
CC consisting of 17 subunits (By similarity). Interacts with POLR3H/RPC8.
CC POLR3H/RPC8 and CRCP/RPC9 probably form a Pol III subcomplex.
CC {ECO:0000250, ECO:0000269|PubMed:12391170,
CC ECO:0000269|PubMed:12482973}.
CC -!- INTERACTION:
CC O75575; Q99081: TCF12; NbExp=3; IntAct=EBI-2654687, EBI-722877;
CC O75575; Q8NF64: ZMIZ2; NbExp=3; IntAct=EBI-2654687, EBI-745786;
CC O75575; Q8NF64-2: ZMIZ2; NbExp=3; IntAct=EBI-2654687, EBI-10182121;
CC O75575-2; O95994: AGR2; NbExp=3; IntAct=EBI-12880830, EBI-712648;
CC O75575-2; Q9NP97: DYNLRB1; NbExp=3; IntAct=EBI-12880830, EBI-372128;
CC O75575-2; O15499: GSC2; NbExp=3; IntAct=EBI-12880830, EBI-19954058;
CC O75575-2; Q5T3J3: LRIF1; NbExp=3; IntAct=EBI-12880830, EBI-473196;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O75575-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75575-2; Sequence=VSP_007538;
CC Name=3;
CC IsoId=O75575-3; Sequence=VSP_043249, VSP_007538;
CC Name=4;
CC IsoId=O75575-4; Sequence=VSP_046273;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Most prevalent in testis.
CC {ECO:0000269|PubMed:10067875}.
CC -!- SIMILARITY: Belongs to the eukaryotic RPC9 RNA polymerase subunit
CC family. {ECO:0000305}.
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DR EMBL; AF073792; AAC25992.1; -; mRNA.
DR EMBL; U51134; AAD05036.1; -; mRNA.
DR EMBL; AK290553; BAF83242.1; -; mRNA.
DR EMBL; AK303737; BAG64710.1; -; mRNA.
DR EMBL; AK311829; BAG34771.1; -; mRNA.
DR EMBL; BP233211; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BX647867; CAI46069.1; -; mRNA.
DR EMBL; AC068533; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471140; EAX07941.1; -; Genomic_DNA.
DR EMBL; BC040107; AAH40107.1; -; mRNA.
DR EMBL; BC105808; AAI05809.1; -; mRNA.
DR CCDS; CCDS47599.1; -. [O75575-2]
DR CCDS; CCDS47600.1; -. [O75575-4]
DR CCDS; CCDS55116.1; -. [O75575-3]
DR CCDS; CCDS5532.1; -. [O75575-1]
DR RefSeq; NP_001035737.1; NM_001040647.1. [O75575-2]
DR RefSeq; NP_001035738.1; NM_001040648.1. [O75575-4]
DR RefSeq; NP_001135886.1; NM_001142414.1. [O75575-3]
DR RefSeq; NP_055293.1; NM_014478.4. [O75575-1]
DR PDB; 7A6H; EM; 3.30 A; D=1-148.
DR PDB; 7AE1; EM; 2.80 A; D=1-148.
DR PDB; 7AE3; EM; 3.10 A; D=1-148.
DR PDB; 7AEA; EM; 3.40 A; D=1-148.
DR PDB; 7AST; EM; 4.00 A; I=1-148.
DR PDB; 7D58; EM; 2.90 A; D=1-148.
DR PDB; 7D59; EM; 3.10 A; D=1-148.
DR PDB; 7DN3; EM; 3.50 A; D=1-148.
DR PDB; 7DU2; EM; 3.35 A; D=1-148.
DR PDB; 7FJI; EM; 3.60 A; D=1-148.
DR PDB; 7FJJ; EM; 3.60 A; D=1-148.
DR PDBsum; 7A6H; -.
DR PDBsum; 7AE1; -.
DR PDBsum; 7AE3; -.
DR PDBsum; 7AEA; -.
DR PDBsum; 7AST; -.
DR PDBsum; 7D58; -.
DR PDBsum; 7D59; -.
DR PDBsum; 7DN3; -.
DR PDBsum; 7DU2; -.
DR PDBsum; 7FJI; -.
DR PDBsum; 7FJJ; -.
DR AlphaFoldDB; O75575; -.
DR SMR; O75575; -.
DR BioGRID; 118121; 85.
DR IntAct; O75575; 18.
DR MINT; O75575; -.
DR STRING; 9606.ENSP00000378736; -.
DR iPTMnet; O75575; -.
DR MetOSite; O75575; -.
DR PhosphoSitePlus; O75575; -.
DR BioMuta; CRCP; -.
DR EPD; O75575; -.
DR jPOST; O75575; -.
DR MassIVE; O75575; -.
DR MaxQB; O75575; -.
DR PaxDb; O75575; -.
DR PeptideAtlas; O75575; -.
DR PRIDE; O75575; -.
DR ProteomicsDB; 2141; -.
DR ProteomicsDB; 50092; -. [O75575-1]
DR ProteomicsDB; 50093; -. [O75575-2]
DR ProteomicsDB; 50094; -. [O75575-3]
DR Antibodypedia; 34815; 108 antibodies from 25 providers.
DR DNASU; 27297; -.
DR Ensembl; ENST00000338592.5; ENSP00000340044.5; ENSG00000241258.7. [O75575-2]
DR Ensembl; ENST00000395326.8; ENSP00000378736.3; ENSG00000241258.7. [O75575-1]
DR Ensembl; ENST00000398684.6; ENSP00000381674.2; ENSG00000241258.7. [O75575-4]
DR Ensembl; ENST00000431089.6; ENSP00000388653.2; ENSG00000241258.7. [O75575-3]
DR GeneID; 27297; -.
DR KEGG; hsa:27297; -.
DR MANE-Select; ENST00000395326.8; ENSP00000378736.3; NM_014478.5; NP_055293.1.
DR UCSC; uc003tus.4; human. [O75575-1]
DR CTD; 27297; -.
DR DisGeNET; 27297; -.
DR GeneCards; CRCP; -.
DR HGNC; HGNC:17888; CRCP.
DR HPA; ENSG00000241258; Low tissue specificity.
DR MIM; 606121; gene.
DR neXtProt; NX_O75575; -.
DR OpenTargets; ENSG00000241258; -.
DR PharmGKB; PA164718123; -.
DR VEuPathDB; HostDB:ENSG00000241258; -.
DR eggNOG; KOG4168; Eukaryota.
DR GeneTree; ENSGT00390000014189; -.
DR HOGENOM; CLU_092529_5_0_1; -.
DR InParanoid; O75575; -.
DR OMA; VMIINLR; -.
DR PhylomeDB; O75575; -.
DR TreeFam; TF323294; -.
DR PathwayCommons; O75575; -.
DR Reactome; R-HSA-1834949; Cytosolic sensors of pathogen-associated DNA.
DR Reactome; R-HSA-73780; RNA Polymerase III Chain Elongation.
DR Reactome; R-HSA-73980; RNA Polymerase III Transcription Termination.
DR Reactome; R-HSA-749476; RNA Polymerase III Abortive And Retractive Initiation.
DR Reactome; R-HSA-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR Reactome; R-HSA-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
DR Reactome; R-HSA-76071; RNA Polymerase III Transcription Initiation From Type 3 Promoter.
DR SignaLink; O75575; -.
DR SIGNOR; O75575; -.
DR BioGRID-ORCS; 27297; 755 hits in 1095 CRISPR screens.
DR ChiTaRS; CRCP; human.
DR GeneWiki; RCP9; -.
DR GenomeRNAi; 27297; -.
DR Pharos; O75575; Tbio.
DR PRO; PR:O75575; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; O75575; protein.
DR Bgee; ENSG00000241258; Expressed in calcaneal tendon and 181 other tissues.
DR ExpressionAtlas; O75575; baseline and differential.
DR Genevisible; O75575; HS.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0009360; C:DNA polymerase III complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005666; C:RNA polymerase III complex; IBA:GO_Central.
DR GO; GO:0001635; F:calcitonin gene-related peptide receptor activity; IEA:Ensembl.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IDA:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:Ensembl.
DR GO; GO:0006383; P:transcription by RNA polymerase III; IDA:UniProtKB.
DR GO; GO:0006384; P:transcription initiation from RNA polymerase III promoter; IBA:GO_Central.
DR Gene3D; 1.20.1250.40; -; 1.
DR InterPro; IPR010997; HRDC-like_sf.
DR InterPro; IPR006590; RNA_pol_Rpb4/RPC9_core.
DR InterPro; IPR005574; Rpb4/RPC9.
DR InterPro; IPR038324; Rpb4/RPC9_sf.
DR InterPro; IPR038846; RPC9.
DR PANTHER; PTHR15561; PTHR15561; 1.
DR Pfam; PF03874; RNA_pol_Rpb4; 1.
DR SMART; SM00657; RPOL4c; 1.
DR SUPFAM; SSF47819; SSF47819; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Antiviral defense; Cell membrane;
KW DNA-directed RNA polymerase; Immunity; Innate immunity; Membrane; Nucleus;
KW Reference proteome; Transcription.
FT CHAIN 1..148
FT /note="DNA-directed RNA polymerase III subunit RPC9"
FT /id="PRO_0000079335"
FT REGION 124..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..13
FT /note="MEVKDANSALLSN -> MQRGDPGEHLGARSWHLGAVGGGGDSCEVKDANSA
FT LLSN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043249"
FT VAR_SEQ 4..80
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16344560"
FT /id="VSP_046273"
FT VAR_SEQ 14..46
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT /id="VSP_007538"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 38..53
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 57..60
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 63..73
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 80..89
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 95..100
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:7D59"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 110..123
FT /evidence="ECO:0007829|PDB:7AE1"
SQ SEQUENCE 148 AA; 16871 MW; 75943BA57A63AF3D CRC64;
MEVKDANSAL LSNYEVFQLL TDLKEQRKES GKNKHSSGQQ NLNTITYETL KYISKTPCRH
QSPEIVREFL TALKSHKLTK AEKLQLLNHR PVTAVEIQLM VEESEERLTE EQIEALLHTV
TSILPAEPEA EQKKNTNSNV AMDEEDPA
