GenomeNet

Database: UniProt
Entry: Q8K368
LinkDB: Q8K368
Original site: Q8K368 
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   13-FEB-2019, entry version 110.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the 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
RT   project: 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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
RT   paralog 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.,
RA   Landers T., Wurm M., Freund M., Neveling K., Hanenberg H.,
RA   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
RT   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.,
RA   Buzovetsky O., Elledge S.J., Pavletich N.P.;
RT   "Structure of the FANCI-FANCD2 complex: insights into the Fanconi
RT   anemia DNA repair pathway.";
RL   Science 333:312-316(2011).
CC   -!- FUNCTION: Plays an essential role in the repair of DNA double-
CC       strand breaks by homologous recombination and in the repair of
CC       interstrand DNA cross-links (ICLs) by promoting FANCD2
CC       monoubiquitination by FANCL and participating in recruitment to
CC       DNA repair sites. Required for maintenance of chromosomal
CC       stability. Specifically binds branched DNA: binds both single-
CC       stranded DNA (ssDNA) and double-stranded DNA (dsDNA). Participates
CC       in S phase and G2 phase checkpoint activation upon DNA damage.
CC   -!- SUBUNIT: Interacts with FANCD2; the interaction is direct.
CC       Interacts with FANCL. Interacts with MTMR15/FAN1. Interacts with
CC       POLN. {ECO:0000250|UniProtKB:Q9NVI1}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Observed in
CC       spots localized in pairs on the sister chromatids of mitotic
CC       chromosome arms and not centromeres, one on each chromatids. These
CC       foci coincide with common fragile sites. They are frequently
CC       interlinked through BLM-associated ultra-fine DNA bridges (By
CC       similarity). {ECO:0000250}.
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         Note=May be produced at very low levels due to a premature stop
CC         codon in the mRNA, leading to nonsense-mediated mRNA decay. No
CC         experimental confirmation available.;
CC       Name=4;
CC         IsoId=Q8K368-4; Sequence=VSP_026074;
CC         Note=No experimental confirmation available.;
CC   -!- DOMAIN: The C-terminal 30 residues are probably required for
CC       function 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
CC       once DNA repair is completed. Monoubiquitination requires the
CC       FANCA-FANCB-FANCC-FANCE-FANCF-FANCG-FANCM complex. Ubiquitination
CC       is required for binding to chromatin, DNA repair, and normal cell
CC       cycle progression. Monoubiquitination is stimulated by DNA-binding
CC       (By similarity). {ECO:0000250}.
CC   -!- PTM: Phosphorylated in response to DNA damage by ATM and/or ATR.
CC       {ECO:0000269|PubMed:17412408}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC39475.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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   UniGene; Mm.349493; -.
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   SMR; Q8K368; -.
DR   BioGrid; 229017; 2.
DR   STRING; 10090.ENSMUSP00000044931; -.
DR   iPTMnet; Q8K368; -.
DR   PhosphoSitePlus; Q8K368; -.
DR   EPD; Q8K368; -.
DR   PaxDb; Q8K368; -.
DR   PeptideAtlas; Q8K368; -.
DR   PRIDE; Q8K368; -.
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   eggNOG; KOG4553; Eukaryota.
DR   eggNOG; ENOG410XSU9; LUCA.
DR   GeneTree; ENSGT00390000005855; -.
DR   HOGENOM; HOG000112497; -.
DR   HOVERGEN; HBG106622; -.
DR   InParanoid; Q8K368; -.
DR   KO; K10895; -.
DR   OMA; MMNFILP; -.
DR   OrthoDB; 169407at2759; -.
DR   PhylomeDB; Q8K368; -.
DR   TreeFam; TF323694; -.
DR   Reactome; R-MMU-6783310; Fanconi Anemia Pathway.
DR   PRO; PR:Q8K368; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   Bgee; ENSMUSG00000039187; Expressed in 140 organ(s), highest expression level in ear.
DR   ExpressionAtlas; Q8K368; baseline and differential.
DR   Genevisible; Q8K368; MM.
DR   GO; GO:0005829; C:cytosol; 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   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; Complete proteome;
KW   DNA damage; DNA repair; Isopeptide bond; Nucleus; Phosphoprotein;
KW   Reference proteome; Ubl conjugation.
FT   CHAIN         1   1330       Fanconi anemia group I protein homolog.
FT                                /FTId=PRO_0000289977.
FT   MOD_RES     555    555       Phosphoserine.
FT                                {ECO:0000269|PubMed:17412408}.
FT   MOD_RES     558    558       Phosphothreonine.
FT                                {ECO:0000269|PubMed:17412408}.
FT   MOD_RES     729    729       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9NVI1}.
FT   MOD_RES     948    948       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9NVI1}.
FT   MOD_RES    1122   1122       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9NVI1}.
FT   CROSSLNK    522    522       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250|UniProtKB:Q9NVI1}.
FT   VAR_SEQ     371    394       SVHSWDHVTQGLIEFGFILMDSYG -> RLVFRYHHVCTFN
FT                                SSELFKSHGNF (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_026072.
FT   VAR_SEQ     395   1330       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_026073.
FT   VAR_SEQ     879   1330       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_026074.
FT   CONFLICT    540    540       L -> W (in Ref. 3; BAC39475).
FT                                {ECO:0000305}.
FT   HELIX         2     11       {ECO:0000244|PDB:3S51}.
FT   HELIX        15     24       {ECO:0000244|PDB:3S51}.
FT   HELIX        29     38       {ECO:0000244|PDB:3S51}.
FT   HELIX        40     44       {ECO:0000244|PDB:3S51}.
FT   HELIX        46     51       {ECO:0000244|PDB:3S51}.
FT   STRAND       56     58       {ECO:0000244|PDB:3S51}.
FT   HELIX        59     78       {ECO:0000244|PDB:3S51}.
FT   HELIX        83     96       {ECO:0000244|PDB:3S51}.
FT   HELIX        97     99       {ECO:0000244|PDB:3S51}.
FT   HELIX       102    117       {ECO:0000244|PDB:3S51}.
FT   TURN        125    128       {ECO:0000244|PDB:3S51}.
FT   HELIX       129    138       {ECO:0000244|PDB:3S51}.
FT   STRAND      145    148       {ECO:0000244|PDB:3S51}.
FT   HELIX       153    166       {ECO:0000244|PDB:3S51}.
FT   TURN        171    173       {ECO:0000244|PDB:3S51}.
FT   HELIX       174    180       {ECO:0000244|PDB:3S51}.
FT   HELIX       181    183       {ECO:0000244|PDB:3S51}.
FT   HELIX       188    202       {ECO:0000244|PDB:3S51}.
FT   HELIX       207    209       {ECO:0000244|PDB:3S51}.
FT   HELIX       210    221       {ECO:0000244|PDB:3S51}.
FT   HELIX       226    248       {ECO:0000244|PDB:3S51}.
FT   HELIX       261    281       {ECO:0000244|PDB:3S51}.
FT   HELIX       283    293       {ECO:0000244|PDB:3S51}.
FT   HELIX       299    304       {ECO:0000244|PDB:3S51}.
FT   HELIX       307    316       {ECO:0000244|PDB:3S51}.
FT   HELIX       320    322       {ECO:0000244|PDB:3S51}.
FT   HELIX       323    344       {ECO:0000244|PDB:3S51}.
FT   HELIX       348    353       {ECO:0000244|PDB:3S51}.
FT   HELIX       360    370       {ECO:0000244|PDB:3S51}.
FT   TURN        371    374       {ECO:0000244|PDB:3S51}.
FT   HELIX       377    393       {ECO:0000244|PDB:3S51}.
FT   TURN        397    399       {ECO:0000244|PDB:3S4W}.
FT   HELIX       413    432       {ECO:0000244|PDB:3S51}.
FT   HELIX       434    436       {ECO:0000244|PDB:3S51}.
FT   HELIX       437    450       {ECO:0000244|PDB:3S51}.
FT   HELIX       457    469       {ECO:0000244|PDB:3S51}.
FT   HELIX       471    474       {ECO:0000244|PDB:3S51}.
FT   HELIX       478    481       {ECO:0000244|PDB:3S51}.
FT   HELIX       482    486       {ECO:0000244|PDB:3S51}.
FT   TURN        487    489       {ECO:0000244|PDB:3S51}.
FT   HELIX       492    506       {ECO:0000244|PDB:3S51}.
FT   HELIX       510    523       {ECO:0000244|PDB:3S51}.
FT   HELIX       529    545       {ECO:0000244|PDB:3S51}.
FT   HELIX       546    549       {ECO:0000244|PDB:3S4W}.
FT   HELIX       555    559       {ECO:0000244|PDB:3S4W}.
FT   TURN        560    562       {ECO:0000244|PDB:3S4W}.
FT   STRAND      566    570       {ECO:0000244|PDB:3S51}.
FT   STRAND      572    574       {ECO:0000244|PDB:3S51}.
FT   HELIX       582    591       {ECO:0000244|PDB:3S51}.
FT   HELIX       592    595       {ECO:0000244|PDB:3S51}.
FT   HELIX       598    614       {ECO:0000244|PDB:3S51}.
FT   HELIX       616    618       {ECO:0000244|PDB:3S51}.
FT   HELIX       619    633       {ECO:0000244|PDB:3S51}.
FT   STRAND      641    644       {ECO:0000244|PDB:3S4W}.
FT   HELIX       647    649       {ECO:0000244|PDB:3S4W}.
FT   STRAND      650    653       {ECO:0000244|PDB:3S51}.
FT   STRAND      656    659       {ECO:0000244|PDB:3S51}.
FT   HELIX       663    679       {ECO:0000244|PDB:3S51}.
FT   HELIX       693    712       {ECO:0000244|PDB:3S51}.
FT   TURN        718    721       {ECO:0000244|PDB:3S4W}.
FT   HELIX       733    759       {ECO:0000244|PDB:3S51}.
FT   HELIX       764    783       {ECO:0000244|PDB:3S51}.
FT   HELIX       806    816       {ECO:0000244|PDB:3S51}.
FT   STRAND      821    823       {ECO:0000244|PDB:3S51}.
FT   HELIX       825    832       {ECO:0000244|PDB:3S51}.
FT   HELIX       836    854       {ECO:0000244|PDB:3S51}.
FT   HELIX       866    884       {ECO:0000244|PDB:3S51}.
FT   HELIX       903    920       {ECO:0000244|PDB:3S51}.
FT   HELIX       923    925       {ECO:0000244|PDB:3S51}.
FT   HELIX       926    932       {ECO:0000244|PDB:3S51}.
FT   TURN        940    944       {ECO:0000244|PDB:3S4W}.
FT   HELIX       946    967       {ECO:0000244|PDB:3S51}.
FT   HELIX       976    988       {ECO:0000244|PDB:3S51}.
FT   HELIX       998   1011       {ECO:0000244|PDB:3S51}.
FT   HELIX      1018   1032       {ECO:0000244|PDB:3S51}.
FT   TURN       1033   1035       {ECO:0000244|PDB:3S51}.
FT   HELIX      1039   1053       {ECO:0000244|PDB:3S51}.
FT   STRAND     1056   1058       {ECO:0000244|PDB:3S4W}.
FT   HELIX      1073   1076       {ECO:0000244|PDB:3S51}.
FT   TURN       1077   1079       {ECO:0000244|PDB:3S51}.
FT   HELIX      1080   1103       {ECO:0000244|PDB:3S51}.
FT   HELIX      1128   1151       {ECO:0000244|PDB:3S51}.
FT   TURN       1156   1158       {ECO:0000244|PDB:3S51}.
FT   HELIX      1159   1184       {ECO:0000244|PDB:3S51}.
FT   TURN       1185   1188       {ECO:0000244|PDB:3S4W}.
FT   HELIX      1193   1199       {ECO:0000244|PDB:3S51}.
FT   HELIX      1202   1205       {ECO:0000244|PDB:3S51}.
FT   HELIX      1207   1221       {ECO:0000244|PDB:3S51}.
FT   HELIX      1249   1269       {ECO:0000244|PDB:3S51}.
FT   STRAND     1270   1272       {ECO:0000244|PDB:3S4W}.
FT   HELIX      1274   1278       {ECO:0000244|PDB:3S51}.
FT   STRAND     1281   1284       {ECO:0000244|PDB:3S4W}.
FT   HELIX      1292   1297       {ECO:0000244|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
//
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