FACD2_MOUSE
ID FACD2_MOUSE Reviewed; 1450 AA.
AC Q80V62; Q9CWC7;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Fanconi anemia group D2 protein homolog;
DE Short=Protein FACD2;
GN Name=Fancd2;
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 MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-422 (ISOFORM 1).
RG The MGC Project Team;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 341-1450 (ISOFORM 1).
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 [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12893777; DOI=10.1101/gad.1103403;
RA Houghtaling S., Timmers C., Noll M., Finegold M.J., Jones S.N., Meyn M.S.,
RA Grompe M.;
RT "Epithelial cancer in Fanconi anemia complementation group D2 (Fancd2)
RT knockout mice.";
RL Genes Dev. 17:2021-2035(2003).
RN [5]
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 [6]
RP X-RAY CRYSTALLOGRAPHY (3.41 ANGSTROMS) OF 33-1415.
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: Required for maintenance of chromosomal stability. Promotes
CC accurate and efficient pairing of homologs during meiosis. Involved in
CC the repair of DNA double-strand breaks, both by homologous
CC recombination and single-strand annealing. May participate in S phase
CC and G2 phase checkpoint activation upon DNA damage. Plays a role in
CC preventing breakage and loss of missegregating chromatin at the end of
CC cell division, particularly after replication stress (By similarity).
CC Promotes BRCA2/FANCD1 loading onto damaged chromatin. May also be
CC involved in B-cell immunoglobulin isotype switching. {ECO:0000250,
CC ECO:0000269|PubMed:12893777}.
CC -!- SUBUNIT: Interacts directly with FANCE and FANCI. Interacts with USP1
CC and MEN1. The ubiquitinated form specifically interacts with BRCA1 and
CC BLM. Both the nonubiquitinated and the monoubiquitinated forms interact
CC with BRCA2; this interaction is mediated by phosphorylated FANCG and
CC the complex also includes XCCR3. The ubiquitinated form specifically
CC interacts with MTMR15/FAN1 (via UBZ-type zinc finger), leading to
CC recruit MTMR15/FAN1 to sites of DNA damage. Interacts with
CC DCLRE1B/Apollo. Interacts with POLN. Interacts with UHRF1 and UHRF2;
CC these interactions promote FANCD2 activation.
CC {ECO:0000250|UniProtKB:Q9BXW9}.
CC -!- INTERACTION:
CC Q80V62; P27661: H2ax; NbExp=2; IntAct=EBI-7268304, EBI-495621;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Concentrates in
CC nuclear foci during S phase and upon genotoxic stress. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q80V62-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80V62-2; Sequence=VSP_013889, VSP_013890;
CC -!- PTM: Monoubiquitinated on Lys-559 during S phase and upon genotoxic
CC stress by FANCL in complex with E2 ligases UBE2T or UBE2W.
CC Deubiquitinated by USP1 as cells enter G2/M, or once DNA repair is
CC completed. Monoubiquitination requires the joint intervention of the
CC FANC core complex, including FANCA, FANCB, FANCC, FANCE, FANCF, FANCG,
CC FANCL and FANCM, and proteins involved in cell cycle checkpoints and
CC DNA repair, including RPA1, ATR, CHEK1 and BRCA1. Ubiquitination is
CC required for binding to chromatin, interaction with BRCA1, BRCA2 and
CC MTMR15/FAN1, DNA repair, and normal cell cycle progression (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated on several sites including Ser-220 and Ser-1399 in
CC response to genotoxic stress. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice display delayed pre- and postnatal
CC development, defects in germ-cell development, and increase incidence
CC of microphthalmia and tumors of epithelial cell origin.
CC {ECO:0000269|PubMed:12893777}.
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DR EMBL; AK019136; BAB31563.1; -; mRNA.
DR EMBL; CK634273; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CN460982; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC042619; AAH42619.1; -; mRNA.
DR CCDS; CCDS20426.1; -. [Q80V62-1]
DR RefSeq; NP_001028416.2; NM_001033244.3. [Q80V62-1]
DR PDB; 3S4W; X-ray; 3.41 A; B=33-1415.
DR PDBsum; 3S4W; -.
DR AlphaFoldDB; Q80V62; -.
DR SMR; Q80V62; -.
DR BioGRID; 229254; 1682.
DR IntAct; Q80V62; 1.
DR MINT; Q80V62; -.
DR STRING; 10090.ENSMUSP00000045667; -.
DR iPTMnet; Q80V62; -.
DR PhosphoSitePlus; Q80V62; -.
DR EPD; Q80V62; -.
DR MaxQB; Q80V62; -.
DR PaxDb; Q80V62; -.
DR PeptideAtlas; Q80V62; -.
DR PRIDE; Q80V62; -.
DR ProteomicsDB; 275847; -. [Q80V62-1]
DR ProteomicsDB; 275848; -. [Q80V62-2]
DR Antibodypedia; 10521; 653 antibodies from 39 providers.
DR Ensembl; ENSMUST00000036340; ENSMUSP00000045667; ENSMUSG00000034023. [Q80V62-1]
DR GeneID; 211651; -.
DR KEGG; mmu:211651; -.
DR UCSC; uc009dgw.2; mouse. [Q80V62-2]
DR UCSC; uc009dgx.2; mouse. [Q80V62-1]
DR CTD; 2177; -.
DR MGI; MGI:2448480; Fancd2.
DR VEuPathDB; HostDB:ENSMUSG00000034023; -.
DR eggNOG; KOG4712; Eukaryota.
DR GeneTree; ENSGT00390000016970; -.
DR HOGENOM; CLU_002068_1_0_1; -.
DR InParanoid; Q80V62; -.
DR OMA; EFFFDIV; -.
DR PhylomeDB; Q80V62; -.
DR TreeFam; TF101106; -.
DR Reactome; R-MMU-6783310; Fanconi Anemia Pathway.
DR BioGRID-ORCS; 211651; 20 hits in 110 CRISPR screens.
DR ChiTaRS; Fancd2; mouse.
DR PRO; PR:Q80V62; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q80V62; protein.
DR Bgee; ENSMUSG00000034023; Expressed in spermatocyte and 151 other tissues.
DR ExpressionAtlas; Q80V62; baseline and differential.
DR Genevisible; Q80V62; MM.
DR GO; GO:0000793; C:condensed chromosome; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:1990391; C:DNA repair complex; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0070182; F:DNA polymerase binding; ISO:MGI.
DR GO; GO:0048854; P:brain morphogenesis; IGI:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:MGI.
DR GO; GO:0034599; P:cellular response to oxidative stress; IGI:MGI.
DR GO; GO:1990918; P:double-strand break repair involved in meiotic recombination; IBA:GO_Central.
DR GO; GO:0007276; P:gamete generation; IMP:MGI.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IMP:MGI.
DR GO; GO:0036297; P:interstrand cross-link repair; IBA:GO_Central.
DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0097150; P:neuronal stem cell population maintenance; IGI:MGI.
DR GO; GO:2000348; P:regulation of CD40 signaling pathway; IMP:MGI.
DR GO; GO:0051090; P:regulation of DNA-binding transcription factor activity; IMP:MGI.
DR GO; GO:0050727; P:regulation of inflammatory response; IMP:MGI.
DR GO; GO:0045589; P:regulation of regulatory T cell differentiation; IMP:MGI.
DR GO; GO:0010332; P:response to gamma radiation; ISO:MGI.
DR CDD; cd11721; FANCD2; 1.
DR InterPro; IPR029448; FANCD2.
DR PANTHER; PTHR32086; PTHR32086; 1.
DR Pfam; PF14631; FancD2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Developmental protein;
KW DNA damage; DNA repair; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..1450
FT /note="Fanconi anemia group D2 protein homolog"
FT /id="PRO_0000087169"
FT REGION 1..289
FT /note="Interaction with FANCE"
FT /evidence="ECO:0000250"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..357
FT /note="Interaction with BRCA2"
FT /evidence="ECO:0000250"
FT REGION 853..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1398..1450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1412..1431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1432..1450
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXW9"
FT MOD_RES 714
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXW9"
FT MOD_RES 1255
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXW9"
FT MOD_RES 1404
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXW9"
FT MOD_RES 1412
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXW9"
FT MOD_RES 1426
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXW9"
FT MOD_RES 1434
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXW9"
FT CROSSLNK 559
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9BXW9"
FT VAR_SEQ 124..129
FT /note="SMGTFY -> RCGEEA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013889"
FT VAR_SEQ 130..1450
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013890"
FT HELIX 45..52
FT /evidence="ECO:0007829|PDB:3S4W"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 72..83
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 87..101
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 105..111
FT /evidence="ECO:0007829|PDB:3S4W"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 133..139
FT /evidence="ECO:0007829|PDB:3S4W"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 144..159
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 170..175
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 187..200
FT /evidence="ECO:0007829|PDB:3S4W"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 206..211
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 213..216
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 222..235
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 240..249
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 254..266
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 275..285
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 292..304
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 336..354
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 356..368
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 369..371
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 378..389
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 391..405
FT /evidence="ECO:0007829|PDB:3S4W"
FT TURN 406..408
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 412..426
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 430..441
FT /evidence="ECO:0007829|PDB:3S4W"
FT STRAND 443..445
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 446..461
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 465..481
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 484..500
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 502..507
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 509..513
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 514..521
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 524..541
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 548..561
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 566..582
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 603..619
FT /evidence="ECO:0007829|PDB:3S4W"
FT STRAND 620..622
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 623..639
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 644..662
FT /evidence="ECO:0007829|PDB:3S4W"
FT STRAND 679..681
FT /evidence="ECO:0007829|PDB:3S4W"
FT STRAND 685..687
FT /evidence="ECO:0007829|PDB:3S4W"
FT STRAND 689..692
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 697..706
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 727..742
FT /evidence="ECO:0007829|PDB:3S4W"
FT TURN 747..749
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 750..752
FT /evidence="ECO:0007829|PDB:3S4W"
FT STRAND 757..759
FT /evidence="ECO:0007829|PDB:3S4W"
FT STRAND 765..768
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 774..797
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 803..827
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 916..919
FT /evidence="ECO:0007829|PDB:3S4W"
FT TURN 920..922
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 928..935
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 960..978
FT /evidence="ECO:0007829|PDB:3S4W"
FT TURN 1001..1004
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 1007..1034
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 1050..1071
FT /evidence="ECO:0007829|PDB:3S4W"
FT TURN 1074..1077
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 1082..1090
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 1105..1117
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 1118..1122
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 1126..1140
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 1149..1160
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 1174..1190
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 1194..1203
FT /evidence="ECO:0007829|PDB:3S4W"
FT TURN 1204..1206
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 1207..1210
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 1226..1244
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 1254..1280
FT /evidence="ECO:0007829|PDB:3S4W"
FT TURN 1281..1283
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 1287..1305
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 1307..1314
FT /evidence="ECO:0007829|PDB:3S4W"
FT TURN 1315..1317
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 1319..1340
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 1344..1346
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 1349..1352
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 1355..1373
FT /evidence="ECO:0007829|PDB:3S4W"
FT HELIX 1379..1387
FT /evidence="ECO:0007829|PDB:3S4W"
SQ SEQUENCE 1450 AA; 163618 MW; B1B9AE5B580AC2E9 CRC64;
MISKRRRLDS EDKENLTEDA SKTMPLSKLA KKSHNSHEVE ENGSVFVKLL KASGLTLKTG
ENQNQLGVDQ VIFQRKLFQA LRKHPAYPKV IEEFVNGLES YTEDSESLRN CLLSCERLQD
EEASMGTFYS KSLIKLLLGI DILQPAIIKM LFEKVPQFLF ESENRDGINM ARLIINQLKW
LDRIVDGKDL TAQMMQLISV APVNLQHDFI TSLPEILGDS QHANVGKELG ELLVQNTSLT
VPILDVFSSL RLDPNFLSKI RQLVMGKLSS VRLEDFPVIV KFLLHSVTDT TSLEVIAELR
ENLNVQQFIL PSRIQASQSK LKSKGLASSS GNQENSDKDC IVLVFDVIKS AIRYEKTISE
AWFKAIERIE SAAEHKALDV VMLLIIYSTS TQTKKGVEKL LRNKIQSDCI QEQLLDSAFS
THYLVLKDIC PSILLLAQTL FHSQDQRIIL FGSLLYKYAF KFFDTYCQQE VVGALVTHVC
SGTEAEVDTA LDVLLELIVL NASAMRLNAA FVKGILDYLE NMSPQQIRKI FCILSTLAFS
QQPGTSNHIQ DDMHLVIRKQ LSSTVFKYKL IGIIGAVTMA GIMAEDRSVP SNSSQRSANV
SSEQRTQVTS LLQLVHSCTE HSPWASSLYY DEFANLIQER KLAPKTLEWV GQTIFNDFQD
AFVVDFCAAP EGDFPFPVKA LYGLEEYSTQ DGIVINLLPL FYQECAKDAS RATSQESSQR
SMSSLCLASH FRLLRLCVAR QHDGNLDEID GLLDCPLFLP DLEPGEKLES MSAKDRSLMC
SLTFLTFNWF REVVNAFCQQ TSPEMKGKVL SRLKDLVELQ GILEKYLAVI PDYVPPFASV
DLDTLDMMPR SSSAVAAKNR NKGKTGGKKQ KADSNKASCS DTLLTEDTSE CDMAPSGRSH
VDKESTGKEG KTFVSLQNYR AFFRELDIEV FSILHSGLVT KFILDTEMHT EATEVVQLGP
AELLFLLEDL SQKLENMLTA PFAKRICCFK NKGRQNIGFS HLHQRSVQDI VHCVVQLLTP
MCNHLENIHN FFQCLGAEHL SADDKARATA QEQHTMACCY QKLLQVLHAL FAWKGFTHQS
KHRLLHSALE VLSNRLKQME QDQPLEELVS QSFSYLQNFH HSVPSFQCGL YLLRLLMALL
EKSAVPNQKK EKLASLAKQL LCRAWPHGEK EKNPTFNDHL HDVLYIYLEH TDNVLKAIEE
ITGVGVPELV SAPKDAASST FPTLTRHTFV IFFRVMMAEL EKTVKGLQAG TAADSQQVHE
EKLLYWNMAV RDFSILLNLM KVFDSYPVLH VCLKYGRRFV EAFLKQCMPL LDFSFRKHRE
DVLSLLQTLQ LNTRLLHHLC GHSKIRQDTR LTKHVPLLKK SLELLVCRVK AMLVLNNCRE
AFWLGTLKNR DLQGEEIISQ DPSSSESNAE DSEDGVTSHV SRNRATEDGE DEASDEQKDQ
DSDESDDSSS
