ID RD23B_MOUSE Reviewed; 416 AA. AC P54728; Q3TUA4; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 24-JAN-2024, entry version 189. DE RecName: Full=UV excision repair protein RAD23 homolog B; DE Short=HR23B; DE Short=mHR23B; DE AltName: Full=XP-C repair-complementing complex 58 kDa protein; DE Short=p58; GN Name=Rad23b; Synonyms=Mhr23b; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/cJ; TISSUE=Testis; RX PubMed=8808275; DOI=10.1006/geno.1996.0004; RA van der Spek P.J., Visser C.E., Hanaoka F., Smit B., Hagemeijer A., RA Bootsma D., Hoeijmakers J.H.J.; RT "Cloning, comparative mapping, and RNA expression of the mouse homologues RT of the Saccharomyces cerevisiae nucleotide excision repair gene RAD23."; RL Genomics 31:20-27(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Embryo, and Head; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary gland; 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 INTERACTION WITH NGLY1. RX PubMed=11562482; DOI=10.1073/pnas.201393498; RA Park H., Suzuki T., Lennarz W.J.; RT "Identification of proteins that interact with mammalian peptide:N- RT glycanase and implicate this hydrolase in the proteasome-dependent pathway RT for protein degradation."; RL Proc. Natl. Acad. Sci. U.S.A. 98:11163-11168(2001). RN [6] RP DISRUPTION PHENOTYPE. RX PubMed=11809813; DOI=10.1128/mcb.22.4.1233-1245.2002; RA Ng J.M., Vrieling H., Sugasawa K., Ooms M.P., Grootegoed J.A., RA Vreeburg J.T., Visser P., Beems R.B., Gorgels T.G., Hanaoka F., RA Hoeijmakers J.H., van der Horst G.T.; RT "Developmental defects and male sterility in mice lacking the ubiquitin- RT like DNA repair gene mHR23B."; RL Mol. Cell. Biol. 22:1233-1245(2002). RN [7] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=12815074; DOI=10.1101/gad.260003; RA Ng J.M., Vermeulen W., van der Horst G.T., Bergink S., Sugasawa K., RA Vrieling H., Hoeijmakers J.H.; RT "A novel regulation mechanism of DNA repair by damage-induced and RAD23- RT dependent stabilization of xeroderma pigmentosum group C protein."; RL Genes Dev. 17:1630-1645(2003). RN [8] RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE. RX PubMed=15336624; DOI=10.1016/j.dnarep.2004.06.010; RA Okuda Y., Nishi R., Ng J.M., Vermeulen W., van der Horst G.T., Mori T., RA Hoeijmakers J.H., Hanaoka F., Sugasawa K.; RT "Relative levels of the two mammalian Rad23 homologs determine composition RT and stability of the xeroderma pigmentosum group C protein complex."; RL DNA Repair 3:1285-1295(2004). RN [9] RP INTERACTION WITH NGLY1. RX PubMed=15358861; DOI=10.1073/pnas.0405663101; RA Katiyar S., Li G., Lennarz W.J.; RT "A complex between peptide:N-glycanase and two proteasome-linked proteins RT suggests a mechanism for the degradation of misfolded glycoproteins."; RL Proc. Natl. Acad. Sci. U.S.A. 101:13774-13779(2004). RN [10] RP INTERACTION WITH NGLY1. RX PubMed=16249333; DOI=10.1073/pnas.0507155102; RA Li G., Zhou X., Zhao G., Schindelin H., Lennarz W.J.; RT "Multiple modes of interaction of the deglycosylation enzyme, mouse peptide RT N-glycanase, with the proteasome."; RL Proc. Natl. Acad. Sci. U.S.A. 102:15809-15814(2005). RN [11] RP ERRATUM OF PUBMED:16249333. RA Li G., Zhou X., Zhao G., Schindelin H., Lennarz W.J.; RL Proc. Natl. Acad. Sci. U.S.A. 103:1153-1153(2006). RN [12] RP FUNCTION IN ERAD, AND INTERACTION WITH AMFR; NGLY1 AND DEGLYCOSYLATED RP PROTEINS. RX PubMed=16709668; DOI=10.1073/pnas.0602747103; RA Li G., Zhao G., Zhou X., Schindelin H., Lennarz W.J.; RT "The AAA ATPase p97 links peptide N-glycanase to the endoplasmic reticulum- RT associated E3 ligase autocrine motility factor receptor."; RL Proc. Natl. Acad. Sci. U.S.A. 103:8348-8353(2006). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 273-332 IN COMPLEX WITH NGLY1. RX PubMed=16500903; DOI=10.1074/jbc.m600137200; RA Zhao G., Zhou X., Wang L., Li G., Kisker C., Lennarz W.J., Schindelin H.; RT "Structure of the mouse peptide N-glycanase-HR23 complex suggests co- RT evolution of the endoplasmic reticulum-associated degradation and DNA RT repair pathways."; RL J. Biol. Chem. 281:13751-13761(2006). CC -!- FUNCTION: Multiubiquitin chain receptor involved in modulation of CC proteasomal degradation. Binds to polyubiquitin chains. Proposed to be CC capable to bind simultaneously to the 26S proteasome and to CC polyubiquitinated substrates and to deliver ubiquitinated proteins to CC the proteasome. May play a role in endoplasmic reticulum-associated CC degradation (ERAD) of misfolded glycoproteins by association with CC PNGase and delivering deglycosylated proteins to the proteasome. CC {ECO:0000269|PubMed:12815074, ECO:0000269|PubMed:15336624, CC ECO:0000269|PubMed:16709668}. CC -!- FUNCTION: Involved in global genome nucleotide excision repair (GG-NER) CC by acting as component of the XPC complex. Cooperatively with Cetn2 CC appears to stabilize Xpc. May protect Xpc from proteasomal degradation CC (By similarity). {ECO:0000250}. CC -!- FUNCTION: The XPC complex is proposed to represent the first factor CC bound at the sites of DNA damage and together with other core CC recognition factors, Xpa, RPA and the TFIIH complex, is part of the CC pre-incision (or initial recognition) complex. The XPC complex CC recognizes a wide spectrum of damaged DNA characterized by distortions CC of the DNA helix such as single-stranded loops, mismatched bubbles or CC single-stranded overhangs. The orientation of XPC complex binding CC appears to be crucial for inducing a productive NER. XPC complex is CC proposed to recognize and to interact with unpaired bases on the CC undamaged DNA strand which is followed by recruitment of the TFIIH CC complex and subsequent scanning for lesions in the opposite strand in a CC 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers CC (CPDs) which are formed upon UV-induced DNA damage esacpe detection by CC the XPC complex due to a low degree of structural perurbation. Instead CC they are detected by the UV-DDB complex which in turn recruits and CC cooperates with the XPC complex in the respective DNA repair. In vitro, CC the Xpc:Rad23b dimer is sufficient to initiate NER; it preferentially CC binds to cisplatin and UV-damaged double-stranded DNA and also binds to CC a variety of chemically and structurally diverse DNA adducts. CC Xpc:Rad23b contacts DNA both 5' and 3' of a cisplatin lesion with a CC preference for the 5' side. Xpc:Rad23bB induces a bend in DNA upon CC binding. Xpc:Rad23b stimulates the activity of DNA glycosylases Tdg and CC Smug1 (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Component of the XPC complex composed of XPC, RAD23B and CC CETN2. Interacts with NGLY1 and PSMC1. Interacts with ATXN3 (By CC similarity). Interacts with AMFR. Interacts with VCP; the interaction CC is indirect and mediated by NGLY1. {ECO:0000250, CC ECO:0000269|PubMed:11562482, ECO:0000269|PubMed:15358861, CC ECO:0000269|PubMed:16249333, ECO:0000269|PubMed:16500903, CC ECO:0000269|PubMed:16709668}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15336624}. Cytoplasm CC {ECO:0000269|PubMed:15336624}. CC -!- DISRUPTION PHENOTYPE: Impaired embryonic development with a 90 % rate CC of intrauterine or neonatal death. Surviving animals display a variety CC of abnormalities, including retarded growth, facial dysmorphology and CC male sterility. The effect on NER competence is reported conflictingly: CC According PubMed:11809813 no change in NER activity is found and CC according PubMed:15336624 a reduced NER activity is seen. Embryonic CC lethal with Rad23a and Rad23b double deficiency. Double deficient cells CC show reduced cell survival upopn UV radiation and reduced steady-state CC level of Xpc indicating a reduced NER capacity. CC {ECO:0000269|PubMed:11809813, ECO:0000269|PubMed:12815074, CC ECO:0000269|PubMed:15336624}. CC -!- SIMILARITY: Belongs to the RAD23 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X92411; CAA63146.1; -; mRNA. DR EMBL; AK150089; BAE29298.1; -; mRNA. DR EMBL; AK160880; BAE36067.1; -; mRNA. DR EMBL; AK160890; BAE36071.1; -; mRNA. DR EMBL; AK160973; BAE36124.1; -; mRNA. DR EMBL; AL683890; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC027747; AAH27747.1; -; mRNA. DR CCDS; CCDS18194.1; -. DR RefSeq; NP_033037.2; NM_009011.4. DR PDB; 2F4M; X-ray; 1.85 A; B=273-332. DR PDB; 2F4O; X-ray; 2.26 A; B=273-332. DR PDBsum; 2F4M; -. DR PDBsum; 2F4O; -. DR AlphaFoldDB; P54728; -. DR SMR; P54728; -. DR BioGRID; 202562; 33. DR CORUM; P54728; -. DR IntAct; P54728; 6. DR STRING; 10090.ENSMUSP00000030134; -. DR iPTMnet; P54728; -. DR PhosphoSitePlus; P54728; -. DR SwissPalm; P54728; -. DR CPTAC; non-CPTAC-3607; -. DR EPD; P54728; -. DR jPOST; P54728; -. DR MaxQB; P54728; -. DR PaxDb; 10090-ENSMUSP00000030134; -. DR PeptideAtlas; P54728; -. DR ProteomicsDB; 254908; -. DR Pumba; P54728; -. DR Antibodypedia; 29324; 608 antibodies from 37 providers. DR DNASU; 19359; -. DR Ensembl; ENSMUST00000030134.9; ENSMUSP00000030134.9; ENSMUSG00000028426.11. DR GeneID; 19359; -. DR KEGG; mmu:19359; -. DR UCSC; uc012dej.1; mouse. DR AGR; MGI:105128; -. DR CTD; 5887; -. DR MGI; MGI:105128; Rad23b. DR VEuPathDB; HostDB:ENSMUSG00000028426; -. DR eggNOG; KOG0011; Eukaryota. DR GeneTree; ENSGT00390000012078; -. DR HOGENOM; CLU_040364_0_1_1; -. DR InParanoid; P54728; -. DR OMA; PHMLEPI; -. DR OrthoDB; 158575at2759; -. DR PhylomeDB; P54728; -. DR TreeFam; TF101216; -. DR Reactome; R-MMU-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle. DR Reactome; R-MMU-5689877; Josephin domain DUBs. DR Reactome; R-MMU-5696394; DNA Damage Recognition in GG-NER. DR Reactome; R-MMU-5696395; Formation of Incision Complex in GG-NER. DR BioGRID-ORCS; 19359; 12 hits in 114 CRISPR screens. DR ChiTaRS; Rad23b; mouse. DR EvolutionaryTrace; P54728; -. DR PRO; PR:P54728; -. DR Proteomes; UP000000589; Chromosome 4. DR RNAct; P54728; Protein. DR Bgee; ENSMUSG00000028426; Expressed in undifferentiated genital tubercle and 271 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW. DR GO; GO:0071942; C:XPC complex; ISS:UniProtKB. DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro. DR GO; GO:0140612; F:DNA damage sensor activity; ISO:MGI. DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; ISO:MGI. DR GO; GO:0070628; F:proteasome binding; IBA:GO_Central. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:MGI. DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:MGI. DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central. DR GO; GO:0098761; P:cellular response to interleukin-7; IDA:MGI. DR GO; GO:0006974; P:DNA damage response; IDA:MGI. DR GO; GO:0048568; P:embryonic organ development; IEA:Ensembl. DR GO; GO:0006289; P:nucleotide-excision repair; ISO:MGI. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central. DR GO; GO:0032434; P:regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:MGI. DR GO; GO:0007283; P:spermatogenesis; IMP:MGI. DR CDD; cd14377; UBA1_Rad23; 1. DR CDD; cd14428; UBA2_HR23B; 1. DR CDD; cd16126; Ubl_HR23B; 1. DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 2. DR Gene3D; 1.10.10.540; XPC-binding domain; 1. DR InterPro; IPR004806; Rad23. DR InterPro; IPR041811; RAD23A/B_UBA1. DR InterPro; IPR006636; STI1_HS-bd. DR InterPro; IPR015940; UBA. DR InterPro; IPR009060; UBA-like_sf. DR InterPro; IPR000626; Ubiquitin-like_dom. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR InterPro; IPR015360; XPC-bd. DR InterPro; IPR036353; XPC-bd_sf. DR NCBIfam; TIGR00601; rad23; 1. DR PANTHER; PTHR10621; UV EXCISION REPAIR PROTEIN RAD23; 1. DR PANTHER; PTHR10621:SF13; UV EXCISION REPAIR PROTEIN RAD23 HOMOLOG B; 1. DR Pfam; PF00627; UBA; 2. DR Pfam; PF00240; ubiquitin; 1. DR Pfam; PF09280; XPC-binding; 1. DR PRINTS; PR01839; RAD23PROTEIN. DR SMART; SM00727; STI1; 1. DR SMART; SM00165; UBA; 2. DR SMART; SM00213; UBQ; 1. DR SUPFAM; SSF46934; UBA-like; 2. DR SUPFAM; SSF54236; Ubiquitin-like; 1. DR SUPFAM; SSF101238; XPC-binding domain; 1. DR PROSITE; PS50030; UBA; 2. DR PROSITE; PS50053; UBIQUITIN_2; 1. DR Genevisible; P54728; MM. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; DNA damage; DNA repair; Nucleus; Phosphoprotein; KW Proteasome; Reference proteome; Repeat; Ubl conjugation pathway. FT CHAIN 1..416 FT /note="UV excision repair protein RAD23 homolog B" FT /id="PRO_0000114907" FT DOMAIN 1..79 FT /note="Ubiquitin-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214" FT DOMAIN 188..228 FT /note="UBA 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212" FT DOMAIN 274..317 FT /note="STI1" FT DOMAIN 371..411 FT /note="UBA 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212" FT REGION 83..175 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 333..356 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 83..104 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 123..139 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 159..175 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 155 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P54727" FT MOD_RES 160 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P54727" FT MOD_RES 174 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q4KMA2" FT MOD_RES 186 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q4KMA2" FT MOD_RES 199 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q4KMA2" FT MOD_RES 202 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q4KMA2" FT CONFLICT 98 FT /note="A -> T (in Ref. 1; CAA63146 and 4; AAH27747)" FT /evidence="ECO:0000305" FT CONFLICT 118 FT /note="P -> A (in Ref. 1; CAA63146 and 4; AAH27747)" FT /evidence="ECO:0000305" FT CONFLICT 127 FT /note="A -> T (in Ref. 1; CAA63146 and 4; AAH27747)" FT /evidence="ECO:0000305" FT CONFLICT 337 FT /note="S -> G (in Ref. 1; CAA63146 and 4; AAH27747)" FT /evidence="ECO:0000305" FT HELIX 275..279 FT /evidence="ECO:0007829|PDB:2F4M" FT HELIX 283..294 FT /evidence="ECO:0007829|PDB:2F4M" FT HELIX 296..298 FT /evidence="ECO:0007829|PDB:2F4M" FT HELIX 299..309 FT /evidence="ECO:0007829|PDB:2F4M" FT HELIX 311..319 FT /evidence="ECO:0007829|PDB:2F4M" FT HELIX 321..328 FT /evidence="ECO:0007829|PDB:2F4M" SQ SEQUENCE 416 AA; 43513 MW; 7440E6A9C8ADF454 CRC64; MQVTLKTLQQ QTFKIDIDPE ETVKALKEKI ESEKGKDAFP VAGQKLIYAG KILSDDTALK EYKIDEKNFV VVMVTKPKAV TTAVPATTQP SSTPSPTAVS SSPAVAAAQA PAPTPALPPT STPASTAPAS TTASSEPAPA GATQPEKPAE KPAQTPVLTS PAPADSTPGD SSRSNLFEDA TSALVTGQSY ENMVTEIMSM GYEREQVIAA LRASFNNPDR AVEYLLMGIP GDRESQAVVD PPPQAVSTGT PQSPAVAAAA ATTTATTTTT SGGHPLEFLR NQPQFQQMRQ IIQQNPSLLP ALLQQIGREN PQLLQQISQH QEHFIQMLNE PVQEAGSQGG GGGGGGGGGG GGGGGIAEAG SGHMNYIQVT PQEKEAIERL KALGFPEGLV IQAYFACEKN ENLAANFLLQ QNFDED //