PADI1_HUMAN
ID PADI1_HUMAN Reviewed; 663 AA.
AC Q9ULC6; A1L4K6; Q70SX6;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Protein-arginine deiminase type-1;
DE EC=3.5.3.15 {ECO:0000269|PubMed:12416996, ECO:0000269|PubMed:27393304, ECO:0000269|PubMed:30044909};
DE AltName: Full=Peptidylarginine deiminase I;
DE AltName: Full=Protein-arginine deiminase type I;
GN Name=PADI1; Synonyms=PAD1, PDI1;
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], CATALYTIC ACTIVITY, FUNCTION, COFACTOR, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Epidermis;
RX PubMed=12416996; DOI=10.1042/bj20020870;
RA Guerrin M., Ishigami A., Mechin M.-C., Nachat R., Valmary S., Sebbag M.,
RA Simon M., Senshu T., Serre G.;
RT "cDNA cloning, gene organization and expression analysis of human
RT peptidylarginine deiminase type I.";
RL Biochem. J. 370:167-174(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15087120; DOI=10.1016/j.gene.2003.12.038;
RA Chavanas S., Mechin M.-C., Takahara H., Kawada A., Nachat R., Serre G.,
RA Simon M.;
RT "Comparative analysis of the mouse and human peptidylarginine deiminase
RT gene clusters reveals highly conserved non-coding segments and a new human
RT gene, PADI6.";
RL Gene 330:19-27(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=30044909; DOI=10.1021/acschembio.8b00578;
RA Nemmara V.V., Tilvawala R., Salinger A.J., Miller L., Nguyen S.H.,
RA Weerapana E., Thompson P.R.;
RT "Citrullination Inactivates Nicotinamide- N-methyltransferase.";
RL ACS Chem. Biol. 13:2663-2672(2018).
RN [7] {ECO:0007744|PDB:5HP5}
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) IN COMPLEX WITH CALCIUM, CATALYTIC
RP ACTIVITY, FUNCTION, COFACTOR, AND SUBUNIT.
RX PubMed=27393304; DOI=10.1016/j.jmb.2016.06.018;
RA Saijo S., Nagai A., Kinjo S., Mashimo R., Akimoto M., Kizawa K.,
RA Yabe-Wada T., Shimizu N., Takahara H., Unno M.;
RT "Monomeric Form of Peptidylarginine Deiminase Type I Revealed by X-ray
RT Crystallography and Small-Angle X-ray Scattering.";
RL J. Mol. Biol. 428:3058-3073(2016).
CC -!- FUNCTION: Catalyzes the deimination of arginine residues of proteins.
CC {ECO:0000269|PubMed:12416996, ECO:0000269|PubMed:27393304,
CC ECO:0000269|PubMed:30044909}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-arginyl-[protein] = L-citrullyl-[protein] + NH4(+);
CC Xref=Rhea:RHEA:18089, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:10588,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29965,
CC ChEBI:CHEBI:83397; EC=3.5.3.15;
CC Evidence={ECO:0000269|PubMed:12416996, ECO:0000269|PubMed:27393304,
CC ECO:0000269|PubMed:30044909};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:12416996, ECO:0000269|PubMed:27393304};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:27393304}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12416996}.
CC -!- TISSUE SPECIFICITY: Detected in epidermal keratinocytes (at protein
CC level). Epidermis, prostate, testis, placenta, spleen and thymus.
CC {ECO:0000269|PubMed:12416996}.
CC -!- SIMILARITY: Belongs to the protein arginine deiminase family.
CC {ECO:0000305}.
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DR EMBL; AB033768; BAA85771.1; -; mRNA.
DR EMBL; AJ549502; CAE47741.1; -; Genomic_DNA.
DR EMBL; AL590644; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471134; EAW94833.1; -; Genomic_DNA.
DR EMBL; BC130574; AAI30575.1; -; mRNA.
DR EMBL; BC136402; AAI36403.1; -; mRNA.
DR CCDS; CCDS178.1; -.
DR RefSeq; NP_037490.2; NM_013358.2.
DR PDB; 5HP5; X-ray; 3.20 A; A/B=1-663.
DR PDBsum; 5HP5; -.
DR AlphaFoldDB; Q9ULC6; -.
DR SMR; Q9ULC6; -.
DR BioGRID; 118980; 12.
DR IntAct; Q9ULC6; 3.
DR STRING; 9606.ENSP00000364620; -.
DR BindingDB; Q9ULC6; -.
DR ChEMBL; CHEMBL1909486; -.
DR DrugBank; DB00155; Citrulline.
DR GuidetoPHARMACOLOGY; 2894; -.
DR iPTMnet; Q9ULC6; -.
DR PhosphoSitePlus; Q9ULC6; -.
DR BioMuta; PADI1; -.
DR DMDM; 56757695; -.
DR jPOST; Q9ULC6; -.
DR MassIVE; Q9ULC6; -.
DR PaxDb; Q9ULC6; -.
DR PeptideAtlas; Q9ULC6; -.
DR PRIDE; Q9ULC6; -.
DR ProteomicsDB; 84982; -.
DR Antibodypedia; 14640; 89 antibodies from 16 providers.
DR DNASU; 29943; -.
DR Ensembl; ENST00000375471.5; ENSP00000364620.4; ENSG00000142623.11.
DR Ensembl; ENST00000631074.2; ENSP00000485803.1; ENSG00000281459.3.
DR GeneID; 29943; -.
DR KEGG; hsa:29943; -.
DR MANE-Select; ENST00000375471.5; ENSP00000364620.4; NM_013358.3; NP_037490.2.
DR UCSC; uc001bah.2; human.
DR CTD; 29943; -.
DR DisGeNET; 29943; -.
DR GeneCards; PADI1; -.
DR HGNC; HGNC:18367; PADI1.
DR HPA; ENSG00000142623; Tissue enriched (esophagus).
DR MIM; 607934; gene.
DR neXtProt; NX_Q9ULC6; -.
DR OpenTargets; ENSG00000142623; -.
DR PharmGKB; PA32899; -.
DR VEuPathDB; HostDB:ENSG00000142623; -.
DR eggNOG; ENOG502QVJA; Eukaryota.
DR GeneTree; ENSGT00940000153217; -.
DR HOGENOM; CLU_021911_0_0_1; -.
DR InParanoid; Q9ULC6; -.
DR OMA; VQKCIDW; -.
DR OrthoDB; 787070at2759; -.
DR PhylomeDB; Q9ULC6; -.
DR TreeFam; TF331952; -.
DR BioCyc; MetaCyc:HS06945-MON; -.
DR BRENDA; 3.5.3.15; 2681.
DR PathwayCommons; Q9ULC6; -.
DR Reactome; R-HSA-3247509; Chromatin modifying enzymes.
DR SignaLink; Q9ULC6; -.
DR BioGRID-ORCS; 29943; 7 hits in 1073 CRISPR screens.
DR ChiTaRS; PADI1; human.
DR GeneWiki; PADI1; -.
DR GenomeRNAi; 29943; -.
DR Pharos; Q9ULC6; Tchem.
DR PRO; PR:Q9ULC6; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9ULC6; protein.
DR Bgee; ENSG00000142623; Expressed in lower esophagus mucosa and 66 other tissues.
DR Genevisible; Q9ULC6; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0004668; F:protein-arginine deiminase activity; IDA:UniProtKB.
DR GO; GO:0036414; P:histone citrullination; IBA:GO_Central.
DR Gene3D; 2.60.40.1700; -; 1.
DR Gene3D; 2.60.40.1860; -; 1.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR004303; PAD.
DR InterPro; IPR013530; PAD_C.
DR InterPro; IPR036556; PAD_central_sf.
DR InterPro; IPR013732; PAD_N.
DR InterPro; IPR038685; PAD_N_sf.
DR InterPro; IPR013733; Prot_Arg_deaminase_cen_dom.
DR PANTHER; PTHR10837; PTHR10837; 1.
DR Pfam; PF03068; PAD; 1.
DR Pfam; PF08527; PAD_M; 1.
DR Pfam; PF08526; PAD_N; 1.
DR PIRSF; PIRSF001247; Protein-arginine_deiminase; 1.
DR SUPFAM; SSF110083; SSF110083; 1.
DR SUPFAM; SSF49503; SSF49503; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cytoplasm; Hydrolase; Metal-binding;
KW Reference proteome.
FT CHAIN 1..663
FT /note="Protein-arginine deiminase type-1"
FT /id="PRO_0000220023"
FT ACT_SITE 645
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J8"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:27393304,
FT ECO:0007744|PDB:5HP5"
FT BINDING 155
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:27393304,
FT ECO:0007744|PDB:5HP5"
FT BINDING 155
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:27393304,
FT ECO:0007744|PDB:5HP5"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:27393304,
FT ECO:0007744|PDB:5HP5"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:27393304,
FT ECO:0007744|PDB:5HP5"
FT BINDING 165
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:27393304,
FT ECO:0007744|PDB:5HP5"
FT BINDING 176
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:27393304,
FT ECO:0007744|PDB:5HP5"
FT BINDING 179
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:27393304,
FT ECO:0007744|PDB:5HP5"
FT BINDING 179
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:27393304,
FT ECO:0007744|PDB:5HP5"
FT BINDING 351
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000305|PubMed:27393304,
FT ECO:0007744|PDB:5HP5"
FT BINDING 353
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000305|PubMed:27393304,
FT ECO:0007744|PDB:5HP5"
FT BINDING 364
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:27393304,
FT ECO:0007744|PDB:5HP5"
FT BINDING 371
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000305|PubMed:27393304,
FT ECO:0007744|PDB:5HP5"
FT BINDING 372
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000305|PubMed:27393304,
FT ECO:0007744|PDB:5HP5"
FT BINDING 375
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000305|PubMed:27393304,
FT ECO:0007744|PDB:5HP5"
FT BINDING 409
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000305|PubMed:27393304,
FT ECO:0007744|PDB:5HP5"
FT BINDING 412
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000305|PubMed:27393304,
FT ECO:0007744|PDB:5HP5"
FT VARIANT 649
FT /note="V -> M (in dbSNP:rs16824215)"
FT /id="VAR_053557"
FT CONFLICT 420
FT /note="V -> G (in Ref. 1; BAA85771)"
FT /evidence="ECO:0000305"
FT CONFLICT 499
FT /note="L -> P (in Ref. 1; BAA85771)"
FT /evidence="ECO:0000305"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 15..20
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 39..53
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 90..97
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 105..121
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:5HP5"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:5HP5"
FT HELIX 175..179
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 180..189
FT /evidence="ECO:0007829|PDB:5HP5"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:5HP5"
FT TURN 205..210
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 211..218
FT /evidence="ECO:0007829|PDB:5HP5"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 246..253
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 263..273
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 280..291
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 303..309
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:5HP5"
FT HELIX 319..331
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 335..339
FT /evidence="ECO:0007829|PDB:5HP5"
FT HELIX 341..344
FT /evidence="ECO:0007829|PDB:5HP5"
FT TURN 351..353
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 354..360
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 365..371
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 376..378
FT /evidence="ECO:0007829|PDB:5HP5"
FT HELIX 381..384
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 392..395
FT /evidence="ECO:0007829|PDB:5HP5"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:5HP5"
FT HELIX 409..411
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 430..435
FT /evidence="ECO:0007829|PDB:5HP5"
FT HELIX 446..454
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 461..464
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 468..470
FT /evidence="ECO:0007829|PDB:5HP5"
FT TURN 473..476
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 477..481
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 483..494
FT /evidence="ECO:0007829|PDB:5HP5"
FT HELIX 495..506
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 507..509
FT /evidence="ECO:0007829|PDB:5HP5"
FT HELIX 528..531
FT /evidence="ECO:0007829|PDB:5HP5"
FT HELIX 536..558
FT /evidence="ECO:0007829|PDB:5HP5"
FT TURN 562..564
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 565..569
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 572..575
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 578..583
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 586..588
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 590..592
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 595..599
FT /evidence="ECO:0007829|PDB:5HP5"
FT HELIX 611..620
FT /evidence="ECO:0007829|PDB:5HP5"
FT HELIX 621..623
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 626..630
FT /evidence="ECO:0007829|PDB:5HP5"
FT TURN 633..636
FT /evidence="ECO:0007829|PDB:5HP5"
FT HELIX 637..639
FT /evidence="ECO:0007829|PDB:5HP5"
FT HELIX 643..646
FT /evidence="ECO:0007829|PDB:5HP5"
FT STRAND 647..651
FT /evidence="ECO:0007829|PDB:5HP5"
FT HELIX 658..660
FT /evidence="ECO:0007829|PDB:5HP5"
SQ SEQUENCE 663 AA; 74666 MW; 4674CEBC03A7E7CA CRC64;
MAPKRVVQLS LKMPTHAVCV VGVEAHVDIH SDVPKGANSF RVSGSSGVEV FMVYNRTRVK
EPIGKARWPL DTDADMVVSV GTASKELKDF KVRVSYFGEQ EDQALGRSVL YLTGVDISLE
VDTGRTGKVK RSQGDKKTWR WGPEGYGAIL LVNCDRDNHR SAEPDLTHSW LMSLADLQDM
SPMLLSCNGP DKLFDSHKLV LNVPFSDSKR VRVFCARGGN SLSDYKQVLG PQCLSYEVER
QPGEQEIKFY VEGLTFPDAD FLGLVSLSVS LVDPGTLPEV TLFTDTVGFR MAPWIMTPNT
QPPEELYVCR VMDTHGSNEK FLEDMSYLTL KANCKLTICP QVENRNDRWI QDEMEFGYIE
APHKSFPVVF DSPRNRGLKD FPYKRILGPD FGYVTREIPL PGPSSLDSFG NLDVSPPVTV
GGTEYPLGRI LIGSSFPKSG GRQMARAVRN FLKAQQVQAP VELYSDWLSV GHVDEFLTFV
PTSDQKGFRL LLASPSACLK LFQEKKEEGY GEAAQFDGLK HQAKRSINEM LADRHLQRDN
LHAQKCIDWN RNVLKRELGL AESDIVDIPQ LFFLKNFYAE AFFPDMVNMV VLGKYLGIPK
PYGPIINGRC CLEEKVQSLL EPLGLHCIFI DDYLSYHELQ GEIHCGTNVR RKPFPFKWWN
MVP
