ID   PRDC1_HUMAN             Reviewed;         225 AA.
AC   Q9NRG1; B7Z1Z3; Q53HA7; Q59EL9; Q5VV18; Q5VV20;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 193.
DE   RecName: Full=Phosphoribosyltransferase domain-containing protein 1;
GN   Name=PRTFDC1; Synonyms=HHGP;
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] (ISOFORM 1).
RC   TISSUE=Liver cancer;
RA   Li Y., Wu T., Xu S., Ren S., Chen Z., Han Z.;
RT   "A novel gene expressed in human liver cancer tissue.";
RL   Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain cortex, and Embryo;
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 MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING
RP   (ISOFORMS 2 AND 3).
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA   Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA   Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA   Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA   Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA   Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA   Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA   Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA   McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA   Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA   Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA   Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA   Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA   Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA   Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA   Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Eye;
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   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH GMP; PHOSPHATE AND
RP   CALCIUM IONS, SUBUNIT, AND ABSENCE OF PHOSPHORIBOSYLTRANSFERASE ACTIVITY.
RX   PubMed=21054786; DOI=10.1111/j.1742-4658.2010.07897.x;
RA   Welin M., Egeblad L., Johansson A., Stenmark P., Wang L., Flodin S.,
RA   Nyman T., Tresaugues L., Kotenyova T., Johansson I., Eriksson S.,
RA   Eklund H., Nordlund P.;
RT   "Structural and functional studies of the human phosphoribosyltransferase
RT   domain containing protein 1.";
RL   FEBS J. 277:4920-4930(2010).
CC   -!- FUNCTION: Has low, barely detectable phosphoribosyltransferase activity
CC       (in vitro). Binds GMP, IMP and alpha-D-5-phosphoribosyl 1-pyrophosphate
CC       (PRPP). Is not expected to contribute to purine metabolism or GMP
CC       salvage.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21054786}.
CC   -!- INTERACTION:
CC       Q9NRG1; Q96F85: CNRIP1; NbExp=3; IntAct=EBI-739759, EBI-958255;
CC       Q9NRG1; Q96G04: EEF2KMT; NbExp=8; IntAct=EBI-739759, EBI-747840;
CC       Q9NRG1; Q7L775: EPM2AIP1; NbExp=6; IntAct=EBI-739759, EBI-6255981;
CC       Q9NRG1; Q8NFF5-2: FLAD1; NbExp=3; IntAct=EBI-739759, EBI-11526128;
CC       Q9NRG1; P46926: GNPDA1; NbExp=3; IntAct=EBI-739759, EBI-749356;
CC       Q9NRG1; P00492: HPRT1; NbExp=11; IntAct=EBI-739759, EBI-748210;
CC       Q9NRG1; Q3B8N2: LGALS9B; NbExp=3; IntAct=EBI-739759, EBI-10240775;
CC       Q9NRG1; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-739759, EBI-739832;
CC       Q9NRG1; Q9BTE3: MCMBP; NbExp=3; IntAct=EBI-739759, EBI-749378;
CC       Q9NRG1; Q9BTE3-2: MCMBP; NbExp=6; IntAct=EBI-739759, EBI-9384556;
CC       Q9NRG1; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-739759, EBI-741158;
CC       Q9NRG1; A0A0B4J2F2: SIK1B; NbExp=3; IntAct=EBI-739759, EBI-22345187;
CC       Q9NRG1; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-739759, EBI-742688;
CC       Q9NRG1; P56279: TCL1A; NbExp=6; IntAct=EBI-739759, EBI-749995;
CC       Q9NRG1; O00534: VWA5A; NbExp=3; IntAct=EBI-739759, EBI-12246480;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9NRG1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NRG1-2; Sequence=VSP_031180;
CC       Name=3;
CC         IsoId=Q9NRG1-3; Sequence=VSP_031179;
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. {ECO:0000305}.
CC   -!- CAUTION: Lacks the conserved active site Asp and has no significant
CC       phosphoribosyltransferase activity. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD93029.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF226056; AAF86956.1; -; mRNA.
DR   EMBL; AK021950; BAB13944.1; -; mRNA.
DR   EMBL; AB209792; BAD93029.1; ALT_INIT; mRNA.
DR   EMBL; AK222674; BAD96394.1; -; mRNA.
DR   EMBL; AK294130; BAH11679.1; -; mRNA.
DR   EMBL; AL157385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL512598; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471072; EAW86120.1; -; Genomic_DNA.
DR   EMBL; BC008662; AAH08662.1; -; mRNA.
DR   CCDS; CCDS60506.1; -. [Q9NRG1-2]
DR   CCDS; CCDS7145.1; -. [Q9NRG1-1]
DR   RefSeq; NP_001269715.1; NM_001282786.1. [Q9NRG1-2]
DR   RefSeq; NP_064585.1; NM_020200.6. [Q9NRG1-1]
DR   PDB; 2JBH; X-ray; 1.70 A; A/B=1-225.
DR   PDBsum; 2JBH; -.
DR   AlphaFoldDB; Q9NRG1; -.
DR   SMR; Q9NRG1; -.
DR   BioGRID; 121276; 39.
DR   IntAct; Q9NRG1; 31.
DR   MINT; Q9NRG1; -.
DR   STRING; 9606.ENSP00000318602; -.
DR   iPTMnet; Q9NRG1; -.
DR   PhosphoSitePlus; Q9NRG1; -.
DR   BioMuta; PRTFDC1; -.
DR   DMDM; 74752920; -.
DR   EPD; Q9NRG1; -.
DR   jPOST; Q9NRG1; -.
DR   MassIVE; Q9NRG1; -.
DR   MaxQB; Q9NRG1; -.
DR   PaxDb; 9606-ENSP00000318602; -.
DR   PeptideAtlas; Q9NRG1; -.
DR   ProteomicsDB; 82352; -. [Q9NRG1-1]
DR   ProteomicsDB; 82353; -. [Q9NRG1-2]
DR   ProteomicsDB; 82354; -. [Q9NRG1-3]
DR   Pumba; Q9NRG1; -.
DR   Antibodypedia; 12431; 294 antibodies from 30 providers.
DR   DNASU; 56952; -.
DR   Ensembl; ENST00000320152.11; ENSP00000318602.5; ENSG00000099256.19. [Q9NRG1-1]
DR   Ensembl; ENST00000376376.3; ENSP00000365556.3; ENSG00000099256.19. [Q9NRG1-3]
DR   Ensembl; ENST00000376378.5; ENSP00000365558.1; ENSG00000099256.19. [Q9NRG1-2]
DR   GeneID; 56952; -.
DR   KEGG; hsa:56952; -.
DR   MANE-Select; ENST00000320152.11; ENSP00000318602.5; NM_020200.7; NP_064585.1.
DR   UCSC; uc001ise.3; human. [Q9NRG1-1]
DR   AGR; HGNC:23333; -.
DR   CTD; 56952; -.
DR   DisGeNET; 56952; -.
DR   GeneCards; PRTFDC1; -.
DR   HGNC; HGNC:23333; PRTFDC1.
DR   HPA; ENSG00000099256; Low tissue specificity.
DR   MIM; 610751; gene.
DR   neXtProt; NX_Q9NRG1; -.
DR   OpenTargets; ENSG00000099256; -.
DR   PharmGKB; PA134888009; -.
DR   VEuPathDB; HostDB:ENSG00000099256; -.
DR   eggNOG; KOG3367; Eukaryota.
DR   GeneTree; ENSGT00940000162225; -.
DR   HOGENOM; CLU_073615_3_0_1; -.
DR   InParanoid; Q9NRG1; -.
DR   OMA; VIFMEDI; -.
DR   OrthoDB; 4216383at2759; -.
DR   PhylomeDB; Q9NRG1; -.
DR   TreeFam; TF313367; -.
DR   PathwayCommons; Q9NRG1; -.
DR   SignaLink; Q9NRG1; -.
DR   BioGRID-ORCS; 56952; 6 hits in 1150 CRISPR screens.
DR   ChiTaRS; PRTFDC1; human.
DR   EvolutionaryTrace; Q9NRG1; -.
DR   GenomeRNAi; 56952; -.
DR   Pharos; Q9NRG1; Tbio.
DR   PRO; PR:Q9NRG1; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; Q9NRG1; Protein.
DR   Bgee; ENSG00000099256; Expressed in corpus callosum and 174 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; TAS:UniProtKB.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR   GO; GO:0006166; P:purine ribonucleoside salvage; IEA:InterPro.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.40.50.2020; -; 1.
DR   InterPro; IPR005904; Hxn_phspho_trans.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   NCBIfam; TIGR01203; HGPRTase; 1.
DR   PANTHER; PTHR43340; HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR43340:SF5; PHOSPHORIBOSYLTRANSFERASE DOMAIN-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF53271; PRTase-like; 1.
DR   Genevisible; Q9NRG1; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Magnesium; Metal-binding;
KW   Nucleotide-binding; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22814378"
FT   CHAIN           2..225
FT                   /note="Phosphoribosyltransferase domain-containing protein
FT                   1"
FT                   /id="PRO_0000318176"
FT   BINDING         141..149
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000269|PubMed:21054786"
FT   BINDING         141
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000305"
FT   BINDING         142
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000305"
FT   BINDING         173
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000269|PubMed:21054786"
FT   BINDING         194..195
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000269|PubMed:21054786"
FT   BINDING         201
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000269|PubMed:21054786"
FT   BINDING         201
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22814378"
FT   VAR_SEQ         114..225
FT                   /note="NDQSMGEMQIIGGDDLSTLAGKNVLIVEDVVGTGRTMKALLSNIEKYKPNMI
FT                   KVASLLVKRTSRSDGFRPDYAGFEIPNLFVVGYALDYNEYFRDLNHICVINEHGKEKYR
FT                   V -> LRARLKRTTICDRGGLAFSQGYMSSCAPLQESPNTLWRGYLQVLIPCFHIRFQL
FT                   PRSEQN (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_031179"
FT   VAR_SEQ         185..225
FT                   /note="YAGFEIPNLFVVGYALDYNEYFRDLNHICVINEHGKEKYRV -> SHMRHQ
FT                   (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_031180"
FT   CONFLICT        39
FT                   /note="L -> W (in Ref. 3; BAD93029)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        65
FT                   /note="G -> R (in Ref. 3; BAD96394)"
FT                   /evidence="ECO:0000305"
FT   HELIX           11..13
FT                   /evidence="ECO:0007829|PDB:2JBH"
FT   HELIX           26..28
FT                   /evidence="ECO:0007829|PDB:2JBH"
FT   HELIX           33..35
FT                   /evidence="ECO:0007829|PDB:2JBH"
FT   STRAND          38..44
FT                   /evidence="ECO:0007829|PDB:2JBH"
FT   HELIX           46..64
FT                   /evidence="ECO:0007829|PDB:2JBH"
FT   STRAND          69..75
FT                   /evidence="ECO:0007829|PDB:2JBH"
FT   TURN            76..78
FT                   /evidence="ECO:0007829|PDB:2JBH"
FT   HELIX           79..95
FT                   /evidence="ECO:0007829|PDB:2JBH"
FT   STRAND          102..109
FT                   /evidence="ECO:0007829|PDB:2JBH"
FT   STRAND          111..113
FT                   /evidence="ECO:0007829|PDB:2JBH"
FT   STRAND          123..127
FT                   /evidence="ECO:0007829|PDB:2JBH"
FT   HELIX           129..132
FT                   /evidence="ECO:0007829|PDB:2JBH"
FT   STRAND          135..147
FT                   /evidence="ECO:0007829|PDB:2JBH"
FT   HELIX           148..158
FT                   /evidence="ECO:0007829|PDB:2JBH"
FT   STRAND          163..173
FT                   /evidence="ECO:0007829|PDB:2JBH"
FT   STRAND          184..190
FT                   /evidence="ECO:0007829|PDB:2JBH"
FT   STRAND          210..215
FT                   /evidence="ECO:0007829|PDB:2JBH"
FT   HELIX           217..222
FT                   /evidence="ECO:0007829|PDB:2JBH"
SQ   SEQUENCE   225 AA;  25674 MW;  CD612C2783AC3071 CRC64;
     MAGSSEEAPD YGRGVVIMDD WPGYDLNLFT YPQHYYGDLE YVLIPHGIIV DRIERLAKDI
     MKDIGYSDIM VLCVLKGGYK FCADLVEHLK NISRNSDRFV SMKVDFIRLK SYRNDQSMGE
     MQIIGGDDLS TLAGKNVLIV EDVVGTGRTM KALLSNIEKY KPNMIKVASL LVKRTSRSDG
     FRPDYAGFEI PNLFVVGYAL DYNEYFRDLN HICVINEHGK EKYRV
//