FANCI_MOUSE
ID FANCI_MOUSE Reviewed; 1330 AA.
AC Q8K368; Q8BUE9; Q8R3G8;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Fanconi anemia group I protein homolog;
DE Short=Protein FACI;
GN Name=Fanci;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 27-1330 (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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 [4]
RP PHOSPHORYLATION AT SER-555 AND THR-558.
RX PubMed=17412408; DOI=10.1016/j.cell.2007.03.009;
RA Smogorzewska A., Matsuoka S., Vinciguerra P., McDonald E.R. III,
RA Hurov K.E., Luo J., Ballif B.A., Gygi S.P., Hofmann K., D'Andrea A.D.,
RA Elledge S.J.;
RT "Identification of the FANCI protein, a monoubiquitinated FANCD2 paralog
RT required for DNA repair.";
RL Cell 129:289-301(2007).
RN [5]
RP IDENTIFICATION.
RX PubMed=17460694; DOI=10.1038/nsmb1252;
RA Sims A.E., Spiteri E., Sims R.J. III, Arita A.G., Lach F.P., Landers T.,
RA Wurm M., Freund M., Neveling K., Hanenberg H., Auerbach A.D., Huang T.T.;
RT "FANCI is a second monoubiquitinated member of the Fanconi anemia
RT pathway.";
RL Nat. Struct. Mol. Biol. 14:564-567(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [7]
RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 1-1302.
RX PubMed=21764741; DOI=10.1126/science.1205805;
RA Joo W., Xu G., Persky N.S., Smogorzewska A., Rudge D.G., Buzovetsky O.,
RA Elledge S.J., Pavletich N.P.;
RT "Structure of the FANCI-FANCD2 complex: insights into the Fanconi anemia
RT DNA repair pathway.";
RL Science 333:312-316(2011).
CC -!- FUNCTION: Plays an essential role in the repair of DNA double-strand
CC breaks by homologous recombination and in the repair of interstrand DNA
CC cross-links (ICLs) by promoting FANCD2 monoubiquitination by FANCL and
CC participating in recruitment to DNA repair sites. Required for
CC maintenance of chromosomal stability. Specifically binds branched DNA:
CC binds both single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA).
CC Participates in S phase and G2 phase checkpoint activation upon DNA
CC damage.
CC -!- SUBUNIT: Interacts with FANCD2; the interaction is direct. Interacts
CC with FANCL. Interacts with MTMR15/FAN1. Interacts with POLN.
CC {ECO:0000250|UniProtKB:Q9NVI1}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NVI1}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9NVI1}. Note=Observed in spots localized in
CC pairs on the sister chromatids of mitotic chromosome arms and not
CC centromeres, one on each chromatids. These foci coincide with common
CC fragile sites. They are frequently interlinked through BLM-associated
CC ultra-fine DNA bridges (By similarity). {ECO:0000250|UniProtKB:Q9NVI1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8K368-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K368-2; Sequence=VSP_026072, VSP_026073;
CC Name=4;
CC IsoId=Q8K368-4; Sequence=VSP_026074;
CC -!- DOMAIN: The C-terminal 30 residues are probably required for function
CC in DNA repair. {ECO:0000250}.
CC -!- PTM: Monoubiquitinated by FANCL on Lys-522 during S phase and upon
CC genotoxic stress. Deubiquitinated by USP1 as cells enter G2/M, or once
CC DNA repair is completed. Monoubiquitination requires the FANCA-FANCB-
CC FANCC-FANCE-FANCF-FANCG-FANCM complex. Ubiquitination is required for
CC binding to chromatin, DNA repair, and normal cell cycle progression.
CC Monoubiquitination is stimulated by DNA-binding (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated in response to DNA damage by ATM and/or ATR.
CC {ECO:0000269|PubMed:17412408}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC39475.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC110909; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC027836; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK085572; BAC39475.1; ALT_INIT; mRNA.
DR CCDS; CCDS39991.1; -. [Q8K368-1]
DR RefSeq; NP_666058.2; NM_145946.2. [Q8K368-1]
DR PDB; 3S4W; X-ray; 3.41 A; A=1-1302.
DR PDB; 3S4Z; X-ray; 7.80 A; A/B/C=1-1302.
DR PDB; 3S51; X-ray; 3.30 A; A/B/C/D=1-1302.
DR PDBsum; 3S4W; -.
DR PDBsum; 3S4Z; -.
DR PDBsum; 3S51; -.
DR AlphaFoldDB; Q8K368; -.
DR SMR; Q8K368; -.
DR BioGRID; 229017; 7.
DR STRING; 10090.ENSMUSP00000044931; -.
DR iPTMnet; Q8K368; -.
DR PhosphoSitePlus; Q8K368; -.
DR EPD; Q8K368; -.
DR MaxQB; Q8K368; -.
DR PaxDb; Q8K368; -.
DR PeptideAtlas; Q8K368; -.
DR PRIDE; Q8K368; -.
DR ProteomicsDB; 267712; -. [Q8K368-1]
DR ProteomicsDB; 267713; -. [Q8K368-2]
DR ProteomicsDB; 267714; -. [Q8K368-4]
DR Antibodypedia; 15714; 144 antibodies from 25 providers.
DR DNASU; 208836; -.
DR Ensembl; ENSMUST00000036865; ENSMUSP00000044931; ENSMUSG00000039187. [Q8K368-1]
DR Ensembl; ENSMUST00000132091; ENSMUSP00000122113; ENSMUSG00000039187. [Q8K368-2]
DR GeneID; 208836; -.
DR KEGG; mmu:208836; -.
DR UCSC; uc009hyh.1; mouse. [Q8K368-1]
DR CTD; 55215; -.
DR MGI; MGI:2384790; Fanci.
DR VEuPathDB; HostDB:ENSMUSG00000039187; -.
DR eggNOG; KOG4553; Eukaryota.
DR GeneTree; ENSGT00390000005855; -.
DR HOGENOM; CLU_700118_0_0_1; -.
DR InParanoid; Q8K368; -.
DR OMA; QHSISGY; -.
DR OrthoDB; 169407at2759; -.
DR PhylomeDB; Q8K368; -.
DR TreeFam; TF323694; -.
DR Reactome; R-MMU-6783310; Fanconi Anemia Pathway.
DR BioGRID-ORCS; 208836; 27 hits in 111 CRISPR screens.
DR ChiTaRS; Fanci; mouse.
DR PRO; PR:Q8K368; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8K368; protein.
DR Bgee; ENSMUSG00000039187; Expressed in ear vesicle and 133 other tissues.
DR ExpressionAtlas; Q8K368; baseline and differential.
DR Genevisible; Q8K368; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:1990391; C:DNA repair complex; ISO:MGI.
DR GO; GO:0043240; C:Fanconi anaemia nuclear complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0070182; F:DNA polymerase binding; ISO:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISO:MGI.
DR CDD; cd11720; FANCI; 1.
DR DisProt; DP02613; -.
DR InterPro; IPR026171; FANCI.
DR InterPro; IPR029310; FANCI_HD1.
DR InterPro; IPR029312; FANCI_HD2.
DR InterPro; IPR029308; FANCI_S1.
DR InterPro; IPR029305; FANCI_S1-cap.
DR InterPro; IPR029315; FANCI_S2.
DR InterPro; IPR029313; FANCI_S3.
DR InterPro; IPR029314; FANCI_S4.
DR PANTHER; PTHR21818; PTHR21818; 1.
DR Pfam; PF14679; FANCI_HD1; 1.
DR Pfam; PF14680; FANCI_HD2; 1.
DR Pfam; PF14675; FANCI_S1; 1.
DR Pfam; PF14674; FANCI_S1-cap; 1.
DR Pfam; PF14676; FANCI_S2; 1.
DR Pfam; PF14677; FANCI_S3; 1.
DR Pfam; PF14678; FANCI_S4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cytoplasm; DNA damage;
KW DNA repair; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..1330
FT /note="Fanconi anemia group I protein homolog"
FT /id="PRO_0000289977"
FT REGION 1299..1330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1308..1324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 555
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17412408"
FT MOD_RES 558
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17412408"
FT MOD_RES 729
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NVI1"
FT MOD_RES 948
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NVI1"
FT MOD_RES 1122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NVI1"
FT CROSSLNK 522
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9NVI1"
FT VAR_SEQ 371..394
FT /note="SVHSWDHVTQGLIEFGFILMDSYG -> RLVFRYHHVCTFNSSELFKSHGNF
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026072"
FT VAR_SEQ 395..1330
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026073"
FT VAR_SEQ 879..1330
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026074"
FT CONFLICT 540
FT /note="L -> W (in Ref. 3; BAC39475)"
FT /evidence="ECO:0000305"
FT HELIX 2..11
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 15..24
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 29..38
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 40..44
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 46..51
FT /evidence="ECO:0007829|PDB:3S51"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 59..78
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 83..96
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 102..117
FT /evidence="ECO:0007829|PDB:3S51"
FT TURN 125..128
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 129..138
FT /evidence="ECO:0007829|PDB:3S51"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 153..166
FT /evidence="ECO:0007829|PDB:3S51"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 174..180
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 188..202
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 210..221
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 226..248
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 261..281
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 283..293
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 299..304
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 307..316
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 323..344
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 348..353
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 360..370
FT /evidence="ECO:0007829|PDB:3S51"
FT TURN 371..374
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 377..393
FT /evidence="ECO:0007829|PDB:3S51"
FT TURN 397..399
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 413..432
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 434..436
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 437..450
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 457..469
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 471..474
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 478..481
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 482..486
FT /evidence="ECO:0007829|PDB:3S51"
FT TURN 487..489
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 492..506
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 510..523
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 529..545
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 546..549
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 555..559
FT /evidence="ECO:0007829|PDB:3S4W"
FT TURN 560..562
FT /evidence="ECO:0007829|PDB:3S4W"
FT STRAND 566..570
FT /evidence="ECO:0007829|PDB:3S51"
FT STRAND 572..574
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 582..591
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 592..595
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 598..614
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 616..618
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 619..633
FT /evidence="ECO:0007829|PDB:3S51"
FT STRAND 641..644
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 647..649
FT /evidence="ECO:0007829|PDB:3S4W"
FT STRAND 650..653
FT /evidence="ECO:0007829|PDB:3S51"
FT STRAND 656..659
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 663..679
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 693..712
FT /evidence="ECO:0007829|PDB:3S51"
FT TURN 718..721
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 733..759
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 764..783
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 806..816
FT /evidence="ECO:0007829|PDB:3S51"
FT STRAND 821..823
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 825..832
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 836..854
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 866..884
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 903..920
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 923..925
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 926..932
FT /evidence="ECO:0007829|PDB:3S51"
FT TURN 940..944
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 946..967
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 976..988
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 998..1011
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 1018..1032
FT /evidence="ECO:0007829|PDB:3S51"
FT TURN 1033..1035
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 1039..1053
FT /evidence="ECO:0007829|PDB:3S51"
FT STRAND 1056..1058
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 1073..1076
FT /evidence="ECO:0007829|PDB:3S51"
FT TURN 1077..1079
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 1080..1103
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 1128..1151
FT /evidence="ECO:0007829|PDB:3S51"
FT TURN 1156..1158
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 1159..1184
FT /evidence="ECO:0007829|PDB:3S51"
FT TURN 1185..1188
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 1193..1199
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 1202..1205
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 1207..1221
FT /evidence="ECO:0007829|PDB:3S51"
FT HELIX 1249..1269
FT /evidence="ECO:0007829|PDB:3S51"
FT STRAND 1270..1272
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 1274..1278
FT /evidence="ECO:0007829|PDB:3S51"
FT STRAND 1281..1284
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 1292..1297
FT /evidence="ECO:0007829|PDB:3S4W"
SQ SEQUENCE 1330 AA; 149326 MW; 68A0580B54E20CBB CRC64;
MDLKILSLAT DKTTDKLQEF LQTLKDDDLA SLLQNQAVKG RAVGTLLRAV LKGSPCSEED
GALRRYKIYS CCIQLVESGD LQQDVASEII GLLMLEVHHF PGPLLVDLAS DFVGAVREDR
LVNGKSLELL PIILTALATK KEVLACGKGD LNGEEYKRQL IDTLCSVRWP QRYMIQLTSV
FKDVCLTPEE MNLVVAKVLT MFSKLNLQEI PPLVYQLLVL SSKGSRRSVL DGIIAFFREL
DKQHREEQSS DELSELITAP ADELYHVEGT VILHIVFAIK LDCELGRELL KHLKAGQQGD
PSKCLCPFSI ALLLSLTRIQ RFEEQVFDLL KTSVVKSFKD LQLLQGSKFL QTLVPQRTCV
STMILEVVRN SVHSWDHVTQ GLIEFGFILM DSYGPKKILD GKAVEIGTSL SKMTNQHACK
LGANILLETF KIHEMIRQEI LEQVLNRVVT RTSSPINHFL DLFSDIIMYA PLILQNCSKV
TETFDYLTFL PLQTVQGLLK AVQPLLKISM SMRDSLILVL RKAMFASQLD ARKSAVAGFL
LLLKNFKVLG SLPSSQCTQS IGVTQVRVDV HSRYSAVANE TFCLEIIDSL KRSLGQQADI
RLMLYDGFYD VLRRNSQLAS SIMQTLFSQL KQFYEPEPDL LPPLKLGACV LTQGSQIFLQ
EPLDHLLSCI QHCLAWYKSR VVPLQQGDEG EEEEEELYSE LDDMLESITV RMIKSELEDF
ELDKSADFSQ NTNVGIKNNI CACLIMGVCE VLMEYNFSIS NFSKSKFEEI LSLFTCYKKF
SDILSEKAGK GKAKMTSKVS DSLLSLKFVS DLLTALFRDS IQSHEESLSV LRSSGEFMHY
AVNVTLQKIQ QLIRTGHVSG PDGQNPDKIF QNLCDITRVL LWRYTSIPTS VEESGKKEKG
KSISLLCLEG LQKTFSVVLQ FYQPKVQQFL QALDVMGTEE EEAGVTVTQR ASFQIRQFQR
SLLNLLSSEE DDFNSKEALL LIAVLSTLSR LLEPTSPQFV QMLSWTSKIC KEYSQEDASF
CKSLMNLFFS LHVLYKSPVT LLRDLSQDIH GQLGDIDQDV EIEKTDHFAV VNLRTAAPTV
CLLVLSQAEK VLEEVDWLIA KIKGSANQET LSDKVTPEDA SSQAVPPTLL IEKAIVMQLG
TLVTFFHELV QTALPSGSCV DTLLKGLSKI YSTLTAFVKY YLQVCQSSRG IPNTVEKLVK
LSGSHLTPVC YSFISYVQNK SSDAPKCSEK EKAAVSTTMA KVLRETKPIP NLVFAIEQYE
KFLIQLSKKS KVNLMQHMKL STSRDFKIKG SVLDMVLRED EEDENEEGTA SAHTQQDREP
AKKRRKKCLS
