RIFK_HUMAN
ID RIFK_HUMAN Reviewed; 155 AA.
AC Q969G6; Q5JSG9; Q9NUT7;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Riboflavin kinase {ECO:0000305|PubMed:19641494};
DE EC=2.7.1.26 {ECO:0000269|PubMed:19641494};
DE AltName: Full=ATP:riboflavin 5'-phosphotransferase;
DE AltName: Full=Flavokinase;
GN Name=RFK;
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 [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Urinary bladder;
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INTERACTION WITH CYBA; TNFRSF1A AND
RP TRADD, AND MUTAGENESIS OF GLU-79.
RX PubMed=19641494; DOI=10.1038/nature08206;
RA Yazdanpanah B., Wiegmann K., Tchikov V., Krut O., Pongratz C., Schramm M.,
RA Kleinridders A., Wunderlich T., Kashkar H., Utermoehlen O., Bruening J.C.,
RA Schuetze S., Kroenke M.;
RT "Riboflavin kinase couples TNF receptor 1 to NADPH oxidase.";
RL Nature 460:1159-1163(2009).
RN [5]
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 [6]
RP X-RAY CRYSTALLOGRAPHY (2.42 ANGSTROMS) OF 1-148 IN COMPLEX WITH ADP; FMN
RP AND MAGNESIUM.
RX PubMed=14580199; DOI=10.1021/bi035450t;
RA Karthikeyan S., Zhou Q., Osterman A.L., Zhang H.;
RT "Ligand binding-induced conformational changes in riboflavin kinase:
RT structural basis for the ordered mechanism.";
RL Biochemistry 42:12532-12538(2003).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 2-148 IN COMPLEX WITH MG-ADP AND
RP RIBOFLAVIN NUCLEOTIDE.
RX PubMed=12623014; DOI=10.1016/s0969-2126(03)00024-8;
RA Karthikeyan S., Zhou Q., Mseeh F., Grishin N.V., Osterman A.L., Zhang H.;
RT "Crystal structure of human riboflavin kinase reveals a beta barrel fold
RT and a novel active site arch.";
RL Structure 11:265-273(2003).
CC -!- FUNCTION: Catalyzes the phosphorylation of riboflavin (vitamin B2) to
CC form flavin-mononucleotide (FMN), hence rate-limiting enzyme in the
CC synthesis of FAD. Essential for TNF-induced reactive oxygen species
CC (ROS) production. Through its interaction with both TNFRSF1A and CYBA,
CC physically and functionally couples TNFRSF1A to NADPH oxidase. TNF-
CC activation of RFK may enhance the incorporation of FAD in NADPH
CC oxidase, a critical step for the assembly and activation of NADPH
CC oxidase. {ECO:0000269|PubMed:19641494}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + riboflavin = ADP + FMN + H(+); Xref=Rhea:RHEA:14357,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57986,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:456216; EC=2.7.1.26;
CC Evidence={ECO:0000269|PubMed:19641494};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14358;
CC Evidence={ECO:0000305|PubMed:19641494};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12623014, ECO:0000269|PubMed:14580199};
CC Note=Zinc or magnesium.;
CC -!- PATHWAY: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin
CC (ATP route): step 1/1. {ECO:0000269|PubMed:19641494}.
CC -!- SUBUNIT: Monomer. Directly interacts with TNFRSF1A death domain.
CC TNFRSF1A-binding may be supported by TRADD. In the absence of TNFRSF1A,
CC interacts with TRADD. Independently of TNFRSF1A, interacts with the
CC NADPH oxidase subunit CYBA. {ECO:0000269|PubMed:12623014,
CC ECO:0000269|PubMed:19641494}.
CC -!- INTERACTION:
CC Q969G6; P19438: TNFRSF1A; NbExp=4; IntAct=EBI-716872, EBI-299451;
CC Q969G6; P19438-1: TNFRSF1A; NbExp=2; IntAct=EBI-716872, EBI-15795644;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in brain, placenta and urinary bladder.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH07069.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA92033.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK002011; BAA92033.1; ALT_INIT; mRNA.
DR EMBL; AL391868; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007069; AAH07069.1; ALT_INIT; mRNA.
DR CCDS; CCDS35044.2; -.
DR RefSeq; NP_060809.3; NM_018339.5.
DR PDB; 1NB0; X-ray; 1.70 A; A=2-148.
DR PDB; 1NB9; X-ray; 1.70 A; A=2-148.
DR PDB; 1P4M; X-ray; 1.80 A; A=2-148.
DR PDB; 1Q9S; X-ray; 2.42 A; A=1-148.
DR PDBsum; 1NB0; -.
DR PDBsum; 1NB9; -.
DR PDBsum; 1P4M; -.
DR PDBsum; 1Q9S; -.
DR AlphaFoldDB; Q969G6; -.
DR SMR; Q969G6; -.
DR BioGRID; 120594; 17.
DR DIP; DIP-60454N; -.
DR IntAct; Q969G6; 5.
DR STRING; 9606.ENSP00000365926; -.
DR DrugBank; DB03247; Flavin mononucleotide.
DR DrugBank; DB00140; Riboflavin.
DR DrugCentral; Q969G6; -.
DR GlyGen; Q969G6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q969G6; -.
DR PhosphoSitePlus; Q969G6; -.
DR BioMuta; RFK; -.
DR DMDM; 209572667; -.
DR EPD; Q969G6; -.
DR jPOST; Q969G6; -.
DR MassIVE; Q969G6; -.
DR MaxQB; Q969G6; -.
DR PaxDb; Q969G6; -.
DR PeptideAtlas; Q969G6; -.
DR PRIDE; Q969G6; -.
DR ProteomicsDB; 75757; -.
DR Antibodypedia; 27259; 156 antibodies from 24 providers.
DR DNASU; 55312; -.
DR Ensembl; ENST00000376736.6; ENSP00000365926.1; ENSG00000135002.12.
DR GeneID; 55312; -.
DR KEGG; hsa:55312; -.
DR MANE-Select; ENST00000376736.6; ENSP00000365926.1; NM_018339.6; NP_060809.3.
DR UCSC; uc004akd.3; human.
DR CTD; 55312; -.
DR DisGeNET; 55312; -.
DR GeneCards; RFK; -.
DR HGNC; HGNC:30324; RFK.
DR HPA; ENSG00000135002; Low tissue specificity.
DR MIM; 613010; gene.
DR neXtProt; NX_Q969G6; -.
DR OpenTargets; ENSG00000135002; -.
DR PharmGKB; PA134916697; -.
DR VEuPathDB; HostDB:ENSG00000135002; -.
DR eggNOG; KOG3110; Eukaryota.
DR GeneTree; ENSGT00390000015537; -.
DR HOGENOM; CLU_048437_3_3_1; -.
DR InParanoid; Q969G6; -.
DR OMA; EVYKMVL; -.
DR OrthoDB; 1534271at2759; -.
DR PhylomeDB; Q969G6; -.
DR TreeFam; TF313786; -.
DR BioCyc; MetaCyc:HS05938-MON; -.
DR BRENDA; 2.7.1.26; 2681.
DR PathwayCommons; Q969G6; -.
DR Reactome; R-HSA-196843; Vitamin B2 (riboflavin) metabolism.
DR SignaLink; Q969G6; -.
DR UniPathway; UPA00276; UER00406.
DR BioGRID-ORCS; 55312; 257 hits in 1045 CRISPR screens.
DR ChiTaRS; RFK; human.
DR EvolutionaryTrace; Q969G6; -.
DR GenomeRNAi; 55312; -.
DR Pharos; Q969G6; Tbio.
DR PRO; PR:Q969G6; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q969G6; protein.
DR Bgee; ENSG00000135002; Expressed in endothelial cell and 216 other tissues.
DR ExpressionAtlas; Q969G6; baseline and differential.
DR Genevisible; Q969G6; HS.
DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008531; F:riboflavin kinase activity; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0009398; P:FMN biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0033864; P:positive regulation of NAD(P)H oxidase activity; IMP:MGI.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IEA:Ensembl.
DR GO; GO:0009231; P:riboflavin biosynthetic process; NAS:UniProtKB.
DR GO; GO:0006771; P:riboflavin metabolic process; IDA:UniProtKB.
DR Gene3D; 2.40.30.30; -; 1.
DR InterPro; IPR023468; Riboflavin_kinase.
DR InterPro; IPR015865; Riboflavin_kinase_bac/euk.
DR InterPro; IPR023465; Riboflavin_kinase_dom_sf.
DR PANTHER; PTHR22749; PTHR22749; 1.
DR Pfam; PF01687; Flavokinase; 1.
DR SMART; SM00904; Flavokinase; 1.
DR SUPFAM; SSF82114; SSF82114; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Flavoprotein; FMN; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome; Transferase; Zinc.
FT CHAIN 1..155
FT /note="Riboflavin kinase"
FT /id="PRO_0000194148"
FT ACT_SITE 79
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:12623014,
FT ECO:0000269|PubMed:14580199, ECO:0007744|PDB:1NB0,
FT ECO:0007744|PDB:1NB9, ECO:0007744|PDB:1P4M,
FT ECO:0007744|PDB:1Q9S"
FT BINDING 21
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:12623014,
FT ECO:0000269|PubMed:14580199, ECO:0007744|PDB:1NB0,
FT ECO:0007744|PDB:1NB9, ECO:0007744|PDB:1P4M,
FT ECO:0007744|PDB:1Q9S"
FT BINDING 27
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:12623014,
FT ECO:0000269|PubMed:14580199, ECO:0007744|PDB:1NB0,
FT ECO:0007744|PDB:1NB9, ECO:0007744|PDB:1P4M,
FT ECO:0007744|PDB:1Q9S"
FT BINDING 27
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:14580199,
FT ECO:0007744|PDB:1Q9S"
FT BINDING 29
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:12623014,
FT ECO:0000269|PubMed:14580199, ECO:0007744|PDB:1NB0,
FT ECO:0007744|PDB:1NB9, ECO:0007744|PDB:1P4M,
FT ECO:0007744|PDB:1Q9S"
FT BINDING 29
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:14580199,
FT ECO:0007744|PDB:1Q9S"
FT BINDING 82
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:12623014,
FT ECO:0000269|PubMed:14580199, ECO:0007744|PDB:1NB0,
FT ECO:0007744|PDB:1NB9, ECO:0007744|PDB:1P4M,
FT ECO:0007744|PDB:1Q9S"
FT BINDING 84
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:12623014,
FT ECO:0000269|PubMed:14580199, ECO:0007744|PDB:1NB0,
FT ECO:0007744|PDB:1NB9, ECO:0007744|PDB:1P4M,
FT ECO:0007744|PDB:1Q9S"
FT BINDING 91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:12623014,
FT ECO:0000269|PubMed:14580199, ECO:0007744|PDB:1NB0,
FT ECO:0007744|PDB:1NB9, ECO:0007744|PDB:1P4M,
FT ECO:0007744|PDB:1Q9S"
FT BINDING 104
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:12623014,
FT ECO:0000269|PubMed:14580199, ECO:0007744|PDB:1NB0,
FT ECO:0007744|PDB:1NB9, ECO:0007744|PDB:1P4M,
FT ECO:0007744|PDB:1Q9S"
FT BINDING 107
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:12623014,
FT ECO:0000269|PubMed:14580199, ECO:0007744|PDB:1NB0,
FT ECO:0007744|PDB:1NB9, ECO:0007744|PDB:1P4M,
FT ECO:0007744|PDB:1Q9S"
FT BINDING 109
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:12623014,
FT ECO:0000269|PubMed:14580199, ECO:0007744|PDB:1NB0,
FT ECO:0007744|PDB:1NB9, ECO:0007744|PDB:1P4M,
FT ECO:0007744|PDB:1Q9S"
FT MUTAGEN 79
FT /note="E->Q: Loss of riboflavin kinase activity. No effect
FT on TNFRSF1A- and CYBA-binding."
FT /evidence="ECO:0000269|PubMed:19641494"
FT CONFLICT 96
FT /note="N -> S (in Ref. 1; BAA92033)"
FT /evidence="ECO:0000305"
FT STRAND 5..11
FT /evidence="ECO:0007829|PDB:1NB0"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:1NB0"
FT HELIX 20..23
FT /evidence="ECO:0007829|PDB:1NB0"
FT HELIX 32..36
FT /evidence="ECO:0007829|PDB:1NB0"
FT STRAND 44..53
FT /evidence="ECO:0007829|PDB:1NB0"
FT STRAND 59..67
FT /evidence="ECO:0007829|PDB:1NB0"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:1NB0"
FT STRAND 76..84
FT /evidence="ECO:0007829|PDB:1NB0"
FT STRAND 93..104
FT /evidence="ECO:0007829|PDB:1NB0"
FT HELIX 112..129
FT /evidence="ECO:0007829|PDB:1NB0"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:1NB0"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:1NB0"
FT HELIX 142..146
FT /evidence="ECO:0007829|PDB:1NB0"
SQ SEQUENCE 155 AA; 17623 MW; 3E038E487E164EBA CRC64;
MRHLPYFCRG QVVRGFGRGS KQLGIPTANF PEQVVDNLPA DISTGIYYGW ASVGSGDVHK
MVVSIGWNPY YKNTKKSMET HIMHTFKEDF YGEILNVAIV GYLRPEKNFD SLESLISAIQ
GDIEEAKKRL ELPEHLKIKE DNFFQVSKSK IMNGH
