PADI3_HUMAN
ID PADI3_HUMAN Reviewed; 664 AA.
AC Q9ULW8; Q58EY7; Q70SX5;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Protein-arginine deiminase type-3;
DE EC=3.5.3.15 {ECO:0000269|PubMed:27866708};
DE AltName: Full=Peptidylarginine deiminase III;
DE AltName: Full=Protein-arginine deiminase type III;
GN Name=PADI3; Synonyms=PAD3, PDI3;
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], AND CHARACTERIZATION.
RC TISSUE=Keratinocyte;
RX PubMed=11069618; DOI=10.1046/j.1523-1747.2000.00131.x;
RA Kanno T., Kawada A., Yamanouchi J., Yosida-Noro C., Yoshiki A.,
RA Shiraiwa M., Kusakabe M., Manabe M., Tezuka T., Takahara H.;
RT "Human peptidylarginine deiminase type III: molecular cloning and
RT nucleotide sequence of the cDNA, properties of the recombinant enzyme, and
RT immunohistochemical localization in human skin.";
RL J. Invest. Dermatol. 115:813-823(2000).
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 MRNA].
RC TISSUE=Brain;
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 VARIANT [LARGE SCALE ANALYSIS] ARG-509.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [6]
RP INVOLVEMENT IN UHS1, VARIANTS UHS1 HIS-112; VAL-294 AND THR-605,
RP CHARACTERIZATION OF VARIANTS UHS1 HIS-112 AND THR-605, SUBCELLULAR
RP LOCATION, CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=27866708; DOI=10.1016/j.ajhg.2016.10.004;
RA Ue Basmanav F.B., Cau L., Tafazzoli A., Mechin M.C., Wolf S., Romano M.T.,
RA Valentin F., Wiegmann H., Huchenq A., Kandil R., Garcia Bartels N.,
RA Kilic A., George S., Ralser D.J., Bergner S., Ferguson D.J.,
RA Oprisoreanu A.M., Wehner M., Thiele H., Altmueller J., Nuernberg P.,
RA Swan D., Houniet D., Buechner A., Weibel L., Wagner N., Grimalt R.,
RA Bygum A., Serre G., Blume-Peytavi U., Sprecher E., Schoch S., Oji V.,
RA Hamm H., Farrant P., Simon M., Betz R.C.;
RT "Mutations in three genes encoding proteins involved in hair shaft
RT formation cause uncombable hair syndrome.";
RL Am. J. Hum. Genet. 99:1292-1304(2016).
CC -!- FUNCTION: Catalyzes the deimination of arginine residues of proteins.
CC {ECO:0000269|PubMed:27866708}.
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:27866708};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC -!- INTERACTION:
CC Q9ULW8; P24539: ATP5PB; NbExp=3; IntAct=EBI-10488185, EBI-1044810;
CC Q9ULW8; O14645: DNALI1; NbExp=3; IntAct=EBI-10488185, EBI-395638;
CC Q9ULW8; Q0VD86: INCA1; NbExp=3; IntAct=EBI-10488185, EBI-6509505;
CC Q9ULW8; O14901: KLF11; NbExp=3; IntAct=EBI-10488185, EBI-948266;
CC Q9ULW8; P27361: MAPK3; NbExp=3; IntAct=EBI-10488185, EBI-73995;
CC Q9ULW8; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-10488185, EBI-2811583;
CC Q9ULW8; Q9ULW8: PADI3; NbExp=4; IntAct=EBI-10488185, EBI-10488185;
CC Q9ULW8; Q04864-2: REL; NbExp=3; IntAct=EBI-10488185, EBI-10829018;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27866708}.
CC -!- TISSUE SPECIFICITY: Hair follicles, and epidermis at very low levels.
CC -!- DISEASE: Uncombable hair syndrome 1 (UHS1) [MIM:191480]: A form of
CC uncombable hair syndrome, a condition characterized by scalp hair that
CC is impossible to comb due to the haphazard arrangement of the hair
CC bundles. A characteristic morphologic feature is a triangular to
CC reniform to heart shape on cross-sections, and a groove, canal or
CC flattening along the entire length of the hair. Most individuals are
CC affected early in childhood and the hair takes on a spun-glass
CC appearance with the hair becoming dry, curly, glossy, lighter in color,
CC and progressively uncombable. The hair growth rate can range from slow
CC to normal, and the condition improves with age. UHS1 inheritance is
CC autosomal dominant. {ECO:0000269|PubMed:27866708}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the protein arginine deiminase family.
CC {ECO:0000305}.
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DR EMBL; AB026831; BAA85974.1; -; mRNA.
DR EMBL; AJ549502; CAE47742.1; -; Genomic_DNA.
DR EMBL; AL590644; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC041592; AAH41592.1; -; mRNA.
DR EMBL; BC109091; AAI09092.1; -; mRNA.
DR EMBL; BC109092; AAI09093.1; -; mRNA.
DR CCDS; CCDS179.1; -.
DR RefSeq; NP_057317.2; NM_016233.2.
DR PDB; 6CE1; X-ray; 2.80 A; A=1-664.
DR PDB; 7D4Y; X-ray; 2.96 A; A/B=1-664.
DR PDB; 7D56; X-ray; 3.17 A; A/B/C=1-664.
DR PDB; 7D5R; X-ray; 3.15 A; A/B=1-664.
DR PDB; 7D5V; X-ray; 2.10 A; A/B=1-664.
DR PDB; 7D8N; X-ray; 2.75 A; A/B=1-664.
DR PDB; 7DAN; X-ray; 3.10 A; A/B/C=1-664.
DR PDBsum; 6CE1; -.
DR PDBsum; 7D4Y; -.
DR PDBsum; 7D56; -.
DR PDBsum; 7D5R; -.
DR PDBsum; 7D5V; -.
DR PDBsum; 7D8N; -.
DR PDBsum; 7DAN; -.
DR AlphaFoldDB; Q9ULW8; -.
DR SMR; Q9ULW8; -.
DR BioGRID; 119686; 60.
DR IntAct; Q9ULW8; 21.
DR STRING; 9606.ENSP00000364609; -.
DR BindingDB; Q9ULW8; -.
DR ChEMBL; CHEMBL1909488; -.
DR DrugBank; DB00155; Citrulline.
DR iPTMnet; Q9ULW8; -.
DR PhosphoSitePlus; Q9ULW8; -.
DR BioMuta; PADI3; -.
DR DMDM; 56757696; -.
DR EPD; Q9ULW8; -.
DR jPOST; Q9ULW8; -.
DR MassIVE; Q9ULW8; -.
DR MaxQB; Q9ULW8; -.
DR PaxDb; Q9ULW8; -.
DR PeptideAtlas; Q9ULW8; -.
DR PRIDE; Q9ULW8; -.
DR ProteomicsDB; 85144; -.
DR TopDownProteomics; Q9ULW8; -.
DR Antibodypedia; 29341; 97 antibodies from 16 providers.
DR DNASU; 51702; -.
DR Ensembl; ENST00000375460.3; ENSP00000364609.3; ENSG00000142619.4.
DR Ensembl; ENST00000625769.1; ENSP00000486702.1; ENSG00000280549.1.
DR GeneID; 51702; -.
DR KEGG; hsa:51702; -.
DR MANE-Select; ENST00000375460.3; ENSP00000364609.3; NM_016233.2; NP_057317.2.
DR UCSC; uc001bai.4; human.
DR CTD; 51702; -.
DR DisGeNET; 51702; -.
DR GeneCards; PADI3; -.
DR HGNC; HGNC:18337; PADI3.
DR HPA; ENSG00000142619; Group enriched (esophagus, urinary bladder).
DR MalaCards; PADI3; -.
DR MIM; 191480; phenotype.
DR MIM; 606755; gene.
DR neXtProt; NX_Q9ULW8; -.
DR OpenTargets; ENSG00000142619; -.
DR Orphanet; 1410; Uncombable hair syndrome.
DR PharmGKB; PA32901; -.
DR VEuPathDB; HostDB:ENSG00000142619; -.
DR eggNOG; ENOG502QVJA; Eukaryota.
DR GeneTree; ENSGT00940000153217; -.
DR HOGENOM; CLU_021911_0_0_1; -.
DR InParanoid; Q9ULW8; -.
DR OMA; RDNCDQH; -.
DR OrthoDB; 787070at2759; -.
DR PhylomeDB; Q9ULW8; -.
DR TreeFam; TF331952; -.
DR BioCyc; MetaCyc:HS06944-MON; -.
DR BRENDA; 3.5.3.15; 2681.
DR PathwayCommons; Q9ULW8; -.
DR Reactome; R-HSA-3247509; Chromatin modifying enzymes.
DR SignaLink; Q9ULW8; -.
DR BioGRID-ORCS; 51702; 11 hits in 1079 CRISPR screens.
DR GeneWiki; PADI3; -.
DR GenomeRNAi; 51702; -.
DR Pharos; Q9ULW8; Tchem.
DR PRO; PR:Q9ULW8; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9ULW8; protein.
DR Bgee; ENSG00000142619; Expressed in lower esophagus mucosa and 33 other tissues.
DR Genevisible; Q9ULW8; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004668; F:protein-arginine deiminase activity; IMP: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; Disease variant; Hydrolase;
KW Reference proteome.
FT CHAIN 1..664
FT /note="Protein-arginine deiminase type-3"
FT /id="PRO_0000220029"
FT VARIANT 52
FT /note="I -> V (in dbSNP:rs3750300)"
FT /id="VAR_020462"
FT VARIANT 112
FT /note="L -> H (in UHS1; forms large aggregates; decreases
FT protein-arginine deiminase activity; dbSNP:rs142129409)"
FT /evidence="ECO:0000269|PubMed:27866708"
FT /id="VAR_078023"
FT VARIANT 171
FT /note="V -> M (in dbSNP:rs2272629)"
FT /id="VAR_020463"
FT VARIANT 294
FT /note="A -> V (in UHS1; forms large aggregates; decreases
FT protein-arginine deiminase activity; dbSNP:rs144080386)"
FT /evidence="ECO:0000269|PubMed:27866708"
FT /id="VAR_078024"
FT VARIANT 509
FT /note="G -> R (in a breast cancer sample; somatic mutation;
FT dbSNP:rs781009577)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035502"
FT VARIANT 582
FT /note="A -> T (in dbSNP:rs34097903)"
FT /id="VAR_053558"
FT VARIANT 605
FT /note="P -> T (in UHS1; forms large aggregates; decreases
FT protein-arginine deiminase activity; dbSNP:rs144944758)"
FT /evidence="ECO:0000269|PubMed:27866708"
FT /id="VAR_078025"
FT VARIANT 618
FT /note="R -> Q (in dbSNP:rs35624745)"
FT /id="VAR_053559"
FT CONFLICT 480
FT /note="A -> V (in Ref. 1; BAA85974)"
FT /evidence="ECO:0000305"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 15..20
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 24..31
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 90..97
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:7DAN"
FT STRAND 105..121
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:7DAN"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:7D8N"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:7D5R"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 180..189
FT /evidence="ECO:0007829|PDB:7D5V"
FT HELIX 191..195
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:7D5V"
FT HELIX 205..208
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:7D5V"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:7D5R"
FT STRAND 225..233
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:7D5V"
FT TURN 242..245
FT /evidence="ECO:0007829|PDB:6CE1"
FT STRAND 246..253
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 263..273
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:6CE1"
FT STRAND 282..293
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 305..310
FT /evidence="ECO:0007829|PDB:7D5V"
FT HELIX 317..330
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 333..336
FT /evidence="ECO:0007829|PDB:7D5V"
FT TURN 348..350
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 351..359
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 362..369
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:7DAN"
FT HELIX 381..384
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 390..394
FT /evidence="ECO:0007829|PDB:7D5V"
FT HELIX 407..409
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 410..412
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 415..418
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 421..423
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 428..432
FT /evidence="ECO:0007829|PDB:7D5V"
FT HELIX 444..453
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 459..462
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 466..468
FT /evidence="ECO:0007829|PDB:7D5V"
FT HELIX 471..473
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 475..479
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 485..492
FT /evidence="ECO:0007829|PDB:7D5V"
FT HELIX 493..505
FT /evidence="ECO:0007829|PDB:7D5V"
FT TURN 506..510
FT /evidence="ECO:0007829|PDB:7D4Y"
FT TURN 514..516
FT /evidence="ECO:0007829|PDB:7D5V"
FT HELIX 528..532
FT /evidence="ECO:0007829|PDB:7D5V"
FT HELIX 535..558
FT /evidence="ECO:0007829|PDB:7D5V"
FT HELIX 563..565
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 566..570
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 573..576
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 579..584
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 587..589
FT /evidence="ECO:0007829|PDB:7D4Y"
FT STRAND 591..593
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 596..600
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 606..611
FT /evidence="ECO:0007829|PDB:6CE1"
FT HELIX 612..621
FT /evidence="ECO:0007829|PDB:7D5V"
FT HELIX 622..624
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 627..631
FT /evidence="ECO:0007829|PDB:7D5V"
FT STRAND 633..635
FT /evidence="ECO:0007829|PDB:6CE1"
FT STRAND 637..641
FT /evidence="ECO:0007829|PDB:7DAN"
FT HELIX 644..647
FT /evidence="ECO:0007829|PDB:7DAN"
FT STRAND 648..652
FT /evidence="ECO:0007829|PDB:7D5V"
FT HELIX 659..661
FT /evidence="ECO:0007829|PDB:7D5V"
SQ SEQUENCE 664 AA; 74743 MW; 90C22A50BF6FD480 CRC64;
MSLQRIVRVS LEHPTSAVCV AGVETLVDIY GSVPEGTEMF EVYGTPGVDI YISPNMERGR
ERADTRRWRF DATLEIIVVM NSPSNDLNDS HVQISYHSSH EPLPLAYAVL YLTCVDISLD
CDLNCEGRQD RNFVDKRQWV WGPSGYGGIL LVNCDRDDPS CDVQDNCDQH VHCLQDLEDM
SVMVLRTQGP AALFDDHKLV LHTSSYDAKR AQVFHICGPE DVCEAYRHVL GQDKVSYEVP
RLHGDEERFF VEGLSFPDAG FTGLISFHVT LLDDSNEDFS ASPIFTDTVV FRVAPWIMTP
STLPPLEVYV CRVRNNTCFV DAVAELARKA GCKLTICPQA ENRNDRWIQD EMELGYVQAP
HKTLPVVFDS PRNGELQDFP YKRILGPDFG YVTREPRDRS VSGLDSFGNL EVSPPVVANG
KEYPLGRILI GGNLPGSSGR RVTQVVRDFL HAQKVQPPVE LFVDWLAVGH VDEFLSFVPA
PDGKGFRMLL ASPGACFKLF QEKQKCGHGR ALLFQGVVDD EQVKTISINQ VLSNKDLINY
NKFVQSCIDW NREVLKRELG LAECDIIDIP QLFKTERKKA TAFFPDLVNM LVLGKHLGIP
KPFGPIINGC CCLEEKVRSL LEPLGLHCTF IDDFTPYHML HGEVHCGTNV CRKPFSFKWW
NMVP
