RD23B_MOUSE
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 03-AUG-2022, entry version 181.
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, Pancreas,
RC 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}.
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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 CPTAC; non-CPTAC-3607; -.
DR EPD; P54728; -.
DR jPOST; P54728; -.
DR MaxQB; P54728; -.
DR PaxDb; P54728; -.
DR PeptideAtlas; P54728; -.
DR PRIDE; P54728; -.
DR ProteomicsDB; 254908; -.
DR Antibodypedia; 29324; 515 antibodies from 37 providers.
DR DNASU; 19359; -.
DR Ensembl; ENSMUST00000030134; ENSMUSP00000030134; ENSMUSG00000028426.
DR GeneID; 19359; -.
DR KEGG; mmu:19359; -.
DR UCSC; uc012dej.1; mouse.
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; MWDEQSA; -.
DR OrthoDB; 1260050at2759; -.
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 109 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 267 other tissues.
DR Genevisible; P54728; MM.
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:0006974; P:cellular response to DNA damage stimulus; IDA:MGI.
DR GO; GO:0098761; P:cellular response to interleukin-7; 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 Gene3D; 1.10.10.540; -; 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 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; SSF101238; SSF101238; 1.
DR SUPFAM; SSF46934; SSF46934; 2.
DR SUPFAM; SSF54236; SSF54236; 1.
DR TIGRFAMs; TIGR00601; rad23; 1.
DR PROSITE; PS50030; UBA; 2.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
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
