RPR1A_HUMAN
ID RPR1A_HUMAN Reviewed; 312 AA.
AC Q96P16; A8KA42; B2RBA3; Q7Z5G8; Q96FY9; Q9NVL4;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Regulation of nuclear pre-mRNA domain-containing protein 1A;
DE AltName: Full=Cyclin-dependent kinase inhibitor 2B-related protein;
DE AltName: Full=p15INK4B-related protein;
GN Name=RPRD1A; Synonyms=P15RS;
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), POSSIBLE FUNCTION, AND INDUCTION.
RX PubMed=12470661; DOI=10.1016/s0006-291x(02)02684-0;
RA Liu J., Liu H., Zhang X., Gao P., Wang J., Hu Z.;
RT "Identification and characterization of P15RS, a novel P15(INK4b) related
RT gene on G1/S progression.";
RL Biochem. Biophys. Res. Commun. 299:880-885(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta, Teratocarcinoma, 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].
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] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-263 (ISOFORM 1).
RC TISSUE=Eye, and Muscle;
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 PROTEIN SEQUENCE OF 2-12; 107-114; 169-186; 230-237; 243-249 AND 283-291,
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma;
RA Bienvenut W.V., Bilsland A.E., Keith W.N.;
RL Submitted (JAN-2010) to UniProtKB.
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [7]
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 [8]
RP IDENTIFICATION IN THE RNA POLYMERASE II COMPLEX, FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=22231121; DOI=10.4161/trns.2.5.17803;
RA Ni Z., Olsen J.B., Guo X., Zhong G., Ruan E.D., Marcon E., Young P.,
RA Guo H., Li J., Moffat J., Emili A., Greenblatt J.F.;
RT "Control of the RNA polymerase II phosphorylation state in promoter regions
RT by CTD interaction domain-containing proteins RPRD1A and RPRD1B.";
RL Transcription 2:237-242(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285, AND IDENTIFICATION BY
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153 AND SER-156, AND
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).
RN [11]
RP VARIANT [LARGE SCALE ANALYSIS] HIS-21.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [12] {ECO:0007744|PDB:4NAC}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-131, FUNCTION, AND INTERACTION
RP WITH POLR2A.
RX PubMed=24399136; DOI=10.1007/s11427-013-4589-7;
RA Mei K., Jin Z., Ren F., Wang Y., Chang Z., Wang X.;
RT "Structural basis for the recognition of RNA polymerase II C-terminal
RT domain by CREPT and p15RS.";
RL Sci. China Life Sci. 57:97-106(2014).
RN [13] {ECO:0007744|PDB:4JXT}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-137, FUNCTION, SUBUNIT, AND
RP MUTAGENESIS OF ASP-65; ARG-106 AND ARG-114.
RX PubMed=24997600; DOI=10.1038/nsmb.2853;
RA Ni Z., Xu C., Guo X., Hunter G.O., Kuznetsova O.V., Tempel W., Marcon E.,
RA Zhong G., Guo H., Kuo W.H., Li J., Young P., Olsen J.B., Wan C.,
RA Loppnau P., El Bakkouri M., Senisterra G.A., He H., Huang H., Sidhu S.S.,
RA Emili A., Murphy S., Mosley A.L., Arrowsmith C.H., Min J., Greenblatt J.F.;
RT "RPRD1A and RPRD1B are human RNA polymerase II C-terminal domain scaffolds
RT for Ser5 dephosphorylation.";
RL Nat. Struct. Mol. Biol. 21:686-695(2014).
CC -!- FUNCTION: Interacts with phosphorylated C-terminal heptapeptide repeat
CC domain (CTD) of the largest RNA polymerase II subunit POLR2A, and
CC participates in dephosphorylation of the CTD by RPAP2. May act as a
CC negative regulator of cyclin-D1 (CCND1) and cyclin-E (CCNE1) in the
CC cell cycle. {ECO:0000269|PubMed:22231121, ECO:0000269|PubMed:24399136,
CC ECO:0000269|PubMed:24997600}.
CC -!- SUBUNIT: May form a heterodimer with RPRD1B (PubMed:24997600).
CC Associates with the RNA polymerase II subunit POLR2A (via CTD
CC phosphorylated at 'Ser-2' and 'Ser-7' of the heptad repeats)
CC (PubMed:22231121, PubMed:24997600, PubMed:24399136).
CC {ECO:0000269|PubMed:22231121, ECO:0000269|PubMed:24399136,
CC ECO:0000269|PubMed:24997600}.
CC -!- INTERACTION:
CC Q96P16; O00505: KPNA3; NbExp=3; IntAct=EBI-1053506, EBI-358297;
CC Q96P16; P24928: POLR2A; NbExp=3; IntAct=EBI-1053506, EBI-295301;
CC Q96P16; Q9NQG5: RPRD1B; NbExp=4; IntAct=EBI-1053506, EBI-747925;
CC Q96P16-1; Q8IXW5: RPAP2; NbExp=3; IntAct=EBI-16112633, EBI-395878;
CC Q96P16-1; Q96P16-1: RPRD1A; NbExp=3; IntAct=EBI-16112633, EBI-16112633;
CC Q96P16-1; Q9NQG5: RPRD1B; NbExp=4; IntAct=EBI-16112633, EBI-747925;
CC Q96P16-3; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-12840198, EBI-6658203;
CC Q96P16-3; O14964: HGS; NbExp=3; IntAct=EBI-12840198, EBI-740220;
CC Q96P16-3; O60341: KDM1A; NbExp=3; IntAct=EBI-12840198, EBI-710124;
CC Q96P16-3; Q17RB8: LONRF1; NbExp=3; IntAct=EBI-12840198, EBI-2341787;
CC Q96P16-3; Q9UBU9: NXF1; NbExp=3; IntAct=EBI-12840198, EBI-398874;
CC Q96P16-3; Q9NQG5: RPRD1B; NbExp=3; IntAct=EBI-12840198, EBI-747925;
CC Q96P16-3; O00560: SDCBP; NbExp=3; IntAct=EBI-12840198, EBI-727004;
CC Q96P16-3; Q86VK4-3: ZNF410; NbExp=3; IntAct=EBI-12840198, EBI-11741890;
CC Q96P16-3; P36508: ZNF76; NbExp=3; IntAct=EBI-12840198, EBI-7254550;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22231121}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96P16-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96P16-3; Sequence=VSP_029531;
CC -!- INDUCTION: Up-regulated in cells overexpressing CDKN2B.
CC {ECO:0000269|PubMed:12470661}.
CC -!- SIMILARITY: Belongs to the UPF0400 (RTT103) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH10136.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AF419845; AAL15972.1; -; mRNA.
DR EMBL; AK001518; BAA91736.1; -; mRNA.
DR EMBL; AK292907; BAF85596.1; -; mRNA.
DR EMBL; AK314569; BAG37150.1; -; mRNA.
DR EMBL; CH471088; EAX01365.1; -; Genomic_DNA.
DR EMBL; CH471088; EAX01366.1; -; Genomic_DNA.
DR EMBL; CH471088; EAX01367.1; -; Genomic_DNA.
DR EMBL; BC000225; AAH00225.2; -; mRNA.
DR EMBL; BC010136; AAH10136.1; ALT_SEQ; mRNA.
DR CCDS; CCDS11917.1; -. [Q96P16-1]
DR CCDS; CCDS77178.1; -. [Q96P16-3]
DR RefSeq; NP_001290340.1; NM_001303411.1. [Q96P16-3]
DR RefSeq; NP_001290341.1; NM_001303412.1. [Q96P16-3]
DR RefSeq; NP_001290342.1; NM_001303413.1.
DR RefSeq; NP_060640.2; NM_018170.4. [Q96P16-1]
DR RefSeq; XP_011524350.1; XM_011526048.1. [Q96P16-1]
DR RefSeq; XP_011524351.1; XM_011526049.1. [Q96P16-3]
DR RefSeq; XP_011524352.1; XM_011526050.1. [Q96P16-3]
DR PDB; 4JXT; X-ray; 1.90 A; A=1-137.
DR PDB; 4NAC; X-ray; 2.00 A; A/B=1-131.
DR PDBsum; 4JXT; -.
DR PDBsum; 4NAC; -.
DR AlphaFoldDB; Q96P16; -.
DR SMR; Q96P16; -.
DR BioGRID; 120494; 166.
DR DIP; DIP-50901N; -.
DR IntAct; Q96P16; 46.
DR MINT; Q96P16; -.
DR STRING; 9606.ENSP00000381984; -.
DR GlyGen; Q96P16; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96P16; -.
DR PhosphoSitePlus; Q96P16; -.
DR BioMuta; RPRD1A; -.
DR DMDM; 74717048; -.
DR EPD; Q96P16; -.
DR jPOST; Q96P16; -.
DR MassIVE; Q96P16; -.
DR MaxQB; Q96P16; -.
DR PaxDb; Q96P16; -.
DR PeptideAtlas; Q96P16; -.
DR PRIDE; Q96P16; -.
DR ProteomicsDB; 77597; -. [Q96P16-1]
DR ProteomicsDB; 77598; -. [Q96P16-3]
DR ABCD; Q96P16; 6 sequenced antibodies.
DR Antibodypedia; 22307; 123 antibodies from 23 providers.
DR DNASU; 55197; -.
DR Ensembl; ENST00000357384.8; ENSP00000349955.4; ENSG00000141425.18. [Q96P16-1]
DR Ensembl; ENST00000399022.9; ENSP00000381984.3; ENSG00000141425.18. [Q96P16-1]
DR Ensembl; ENST00000588737.5; ENSP00000465444.1; ENSG00000141425.18. [Q96P16-3]
DR Ensembl; ENST00000590898.5; ENSP00000467991.1; ENSG00000141425.18. [Q96P16-3]
DR GeneID; 55197; -.
DR KEGG; hsa:55197; -.
DR MANE-Select; ENST00000399022.9; ENSP00000381984.3; NM_018170.5; NP_060640.2.
DR UCSC; uc002kze.2; human. [Q96P16-1]
DR CTD; 55197; -.
DR DisGeNET; 55197; -.
DR GeneCards; RPRD1A; -.
DR HGNC; HGNC:25560; RPRD1A.
DR HPA; ENSG00000141425; Low tissue specificity.
DR MIM; 610347; gene.
DR neXtProt; NX_Q96P16; -.
DR OpenTargets; ENSG00000141425; -.
DR PharmGKB; PA162402042; -.
DR VEuPathDB; HostDB:ENSG00000141425; -.
DR eggNOG; KOG2669; Eukaryota.
DR GeneTree; ENSGT00950000183094; -.
DR HOGENOM; CLU_055523_1_0_1; -.
DR InParanoid; Q96P16; -.
DR OMA; MAYNDDA; -.
DR PhylomeDB; Q96P16; -.
DR TreeFam; TF320926; -.
DR PathwayCommons; Q96P16; -.
DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR SignaLink; Q96P16; -.
DR BioGRID-ORCS; 55197; 40 hits in 1082 CRISPR screens.
DR ChiTaRS; RPRD1A; human.
DR GenomeRNAi; 55197; -.
DR Pharos; Q96P16; Tbio.
DR PRO; PR:Q96P16; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q96P16; protein.
DR Bgee; ENSG00000141425; Expressed in Brodmann (1909) area 23 and 198 other tissues.
DR ExpressionAtlas; Q96P16; baseline and differential.
DR Genevisible; Q96P16; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016591; C:RNA polymerase II, holoenzyme; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000993; F:RNA polymerase II complex binding; IBA:GO_Central.
DR GO; GO:0070940; P:dephosphorylation of RNA polymerase II C-terminal domain; IMP:UniProtKB.
DR GO; GO:0031124; P:mRNA 3'-end processing; IBA:GO_Central.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR006569; CID_dom.
DR InterPro; IPR032337; CREPT.
DR InterPro; IPR008942; ENTH_VHS.
DR Pfam; PF04818; CID; 1.
DR Pfam; PF16566; CREPT; 1.
DR SMART; SM00582; RPR; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR PROSITE; PS51391; CID; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Coiled coil;
KW Direct protein sequencing; Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330"
FT CHAIN 2..312
FT /note="Regulation of nuclear pre-mRNA domain-containing
FT protein 1A"
FT /id="PRO_0000311344"
FT DOMAIN 2..133
FT /note="CID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00724"
FT COILED 244..286
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..51
FT /note="MSAFSEAALEKKLSELSNSQQSVQTLSLWLIHHRKHSRPIVTVWERELRKA
FT -> MRNSNWRFCQTGIYS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_029531"
FT VARIANT 21
FT /note="Q -> H (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_037229"
FT MUTAGEN 65
FT /note="D->A: Partial loss of binding to POLR2A CTD in
FT vitro."
FT /evidence="ECO:0000269|PubMed:24997600"
FT MUTAGEN 106
FT /note="R->A: Partial loss of binding to POLR2A CTD
FT phosphorylated at 'Ser-2' in the heptad repeats in vitro."
FT /evidence="ECO:0000269|PubMed:24997600"
FT MUTAGEN 114
FT /note="R->A: Partial loss of binding to POLR2A CTD in
FT vitro."
FT /evidence="ECO:0000269|PubMed:24997600"
FT CONFLICT 193
FT /note="E -> D (in Ref. 2; BAA91736)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="I -> V (in Ref. 2; BAA91736)"
FT /evidence="ECO:0000305"
FT HELIX 6..15
FT /evidence="ECO:0007829|PDB:4JXT"
FT HELIX 20..32
FT /evidence="ECO:0007829|PDB:4JXT"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:4JXT"
FT HELIX 37..50
FT /evidence="ECO:0007829|PDB:4JXT"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:4JXT"
FT HELIX 56..70
FT /evidence="ECO:0007829|PDB:4JXT"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:4JXT"
FT HELIX 76..95
FT /evidence="ECO:0007829|PDB:4JXT"
FT HELIX 98..113
FT /evidence="ECO:0007829|PDB:4JXT"
FT HELIX 119..130
FT /evidence="ECO:0007829|PDB:4JXT"
SQ SEQUENCE 312 AA; 35720 MW; 61785281F31CB328 CRC64;
MSAFSEAALE KKLSELSNSQ QSVQTLSLWL IHHRKHSRPI VTVWERELRK AKPNRKLTFL
YLANDVIQNS KRKGPEFTKD FAPVIVEAFK HVSSETDESC KKHLGRVLSI WEERSVYEND
VLEQLKQALY GDKKPRKRTY EQIKVDENEN CSSLGSPSEP PQTLDLVRAL QDLENAASGD
AAVHQRIASL PVEVQEVSLL DKITDKESGE RLSKMVEDAC MLLADYNGRL AAEIDDRKQL
TRMLADFLRC QKEALAEKEH KLEEYKRKLA RVSLVRKELR SRIQSLPDLS RLPNVTGSHM
HLPFAGDIYS ED
