GenomeNet

Database: UniProt
Entry: Q80V62
LinkDB: Q80V62
Original site: Q80V62 
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   13-FEB-2019, entry version 126.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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.,
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   [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
RT   project: 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.,
RA   Meyn M.S., 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
RT   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.,
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: Required for maintenance of chromosomal stability.
CC       Promotes accurate and efficient pairing of homologs during
CC       meiosis. Involved in the repair of DNA double-strand breaks, both
CC       by homologous recombination and single-strand annealing. May
CC       participate in S phase and G2 phase checkpoint activation upon DNA
CC       damage. Plays a role in preventing breakage and loss of
CC       missegregating chromatin at the end of cell division, particularly
CC       after replication stress (By similarity). Promotes BRCA2/FANCD1
CC       loading onto damaged chromatin. May also be involved in B-cell
CC       immunoglobulin isotype switching. {ECO:0000250,
CC       ECO:0000269|PubMed:12893777}.
CC   -!- SUBUNIT: Interacts directly with FANCE and FANCI. Interacts with
CC       USP1 and MEN1. The ubiquitinated form specifically interacts with
CC       BRCA1 and BLM. Both the nonubiquitinated and the monoubiquitinated
CC       forms interact with BRCA2; this interaction is mediated by
CC       phosphorylated FANCG and the complex also includes XCCR3. The
CC       ubiquitinated form specifically interacts with MTMR15/FAN1 (via
CC       UBZ-type zinc finger), leading to recruit MTMR15/FAN1 to sites of
CC       DNA damage. Interacts with DCLRE1B/Apollo. Interacts with POLN.
CC       {ECO:0000250|UniProtKB:Q9BXW9}.
CC   -!- INTERACTION:
CC       P27661:H2afx; 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.
CC       {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
CC       genotoxic stress by FANCL in complex with E2 ligases UBE2T or
CC       UBE2W. Deubiquitinated by USP1 as cells enter G2/M, or once DNA
CC       repair is completed. Monoubiquitination requires the joint
CC       intervention of the FANC core complex, including FANCA, FANCB,
CC       FANCC, FANCE, FANCF, FANCG, FANCL and FANCM, and proteins involved
CC       in cell cycle checkpoints and DNA repair, including RPA1, ATR,
CC       CHEK1 and BRCA1. Ubiquitination is required for binding to
CC       chromatin, interaction with BRCA1, BRCA2 and MTMR15/FAN1, DNA
CC       repair, and normal cell cycle progression (By similarity).
CC       {ECO:0000250}.
CC   -!- PTM: Phosphorylated on several sites including Ser-220 and Ser-
CC       1399 in response to genotoxic stress. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Mice display delayed pre- and postnatal
CC       development, defects in germ-cell development, and increase
CC       incidence of microphthalmia and tumors of epithelial cell origin.
CC       {ECO:0000269|PubMed:12893777}.
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   UniGene; Mm.160061; -.
DR   PDB; 3S4W; X-ray; 3.41 A; B=33-1415.
DR   PDBsum; 3S4W; -.
DR   ProteinModelPortal; Q80V62; -.
DR   SMR; Q80V62; -.
DR   BioGrid; 229254; 1675.
DR   IntAct; Q80V62; 1.
DR   MINT; Q80V62; -.
DR   STRING; 10090.ENSMUSP00000045667; -.
DR   iPTMnet; Q80V62; -.
DR   PhosphoSitePlus; Q80V62; -.
DR   EPD; Q80V62; -.
DR   PaxDb; Q80V62; -.
DR   PeptideAtlas; Q80V62; -.
DR   PRIDE; Q80V62; -.
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   eggNOG; KOG4712; Eukaryota.
DR   eggNOG; ENOG410XT6B; LUCA.
DR   GeneTree; ENSGT00390000016970; -.
DR   HOGENOM; HOG000060189; -.
DR   HOVERGEN; HBG060904; -.
DR   InParanoid; Q80V62; -.
DR   KO; K10891; -.
DR   OMA; NFLMIDF; -.
DR   OrthoDB; 979208at2759; -.
DR   PhylomeDB; Q80V62; -.
DR   TreeFam; TF101106; -.
DR   Reactome; R-MMU-6783310; Fanconi Anemia Pathway.
DR   PRO; PR:Q80V62; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   Bgee; ENSMUSG00000034023; Expressed in 155 organ(s), highest expression level in bone marrow.
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:0016604; C:nuclear body; ISO:MGI.
DR   GO; GO:0005730; C:nucleolus; 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:0006281; P:DNA repair; IBA:GO_Central.
DR   GO; GO:0007276; P:gamete generation; IMP:MGI.
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   GO; GO:0007129; P:synapsis; IMP: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; Complete proteome;
KW   Developmental protein; DNA damage; DNA repair; Isopeptide bond;
KW   Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT   CHAIN         1   1450       Fanconi anemia group D2 protein homolog.
FT                                /FTId=PRO_0000087169.
FT   REGION        1    289       Interaction with FANCE. {ECO:0000250}.
FT   REGION      246    357       Interaction with BRCA2. {ECO:0000250}.
FT   MOD_RES     220    220       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9BXW9}.
FT   MOD_RES     714    714       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9BXW9}.
FT   MOD_RES    1255   1255       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9BXW9}.
FT   MOD_RES    1404   1404       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9BXW9}.
FT   MOD_RES    1412   1412       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9BXW9}.
FT   MOD_RES    1426   1426       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9BXW9}.
FT   MOD_RES    1434   1434       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9BXW9}.
FT   CROSSLNK    559    559       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250|UniProtKB:Q9BXW9}.
FT   VAR_SEQ     124    129       SMGTFY -> RCGEEA (in isoform 2).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_013889.
FT   VAR_SEQ     130   1450       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_013890.
FT   HELIX        45     52       {ECO:0000244|PDB:3S4W}.
FT   STRAND       65     68       {ECO:0000244|PDB:3S4W}.
FT   HELIX        72     83       {ECO:0000244|PDB:3S4W}.
FT   HELIX        87    101       {ECO:0000244|PDB:3S4W}.
FT   HELIX       105    111       {ECO:0000244|PDB:3S4W}.
FT   STRAND      112    114       {ECO:0000244|PDB:3S4W}.
FT   HELIX       133    139       {ECO:0000244|PDB:3S4W}.
FT   TURN        141    143       {ECO:0000244|PDB:3S4W}.
FT   HELIX       144    159       {ECO:0000244|PDB:3S4W}.
FT   HELIX       170    175       {ECO:0000244|PDB:3S4W}.
FT   HELIX       176    178       {ECO:0000244|PDB:3S4W}.
FT   HELIX       187    200       {ECO:0000244|PDB:3S4W}.
FT   TURN        203    205       {ECO:0000244|PDB:3S4W}.
FT   HELIX       206    211       {ECO:0000244|PDB:3S4W}.
FT   HELIX       213    216       {ECO:0000244|PDB:3S4W}.
FT   HELIX       219    221       {ECO:0000244|PDB:3S4W}.
FT   HELIX       222    235       {ECO:0000244|PDB:3S4W}.
FT   HELIX       240    249       {ECO:0000244|PDB:3S4W}.
FT   HELIX       254    266       {ECO:0000244|PDB:3S4W}.
FT   HELIX       275    285       {ECO:0000244|PDB:3S4W}.
FT   HELIX       292    304       {ECO:0000244|PDB:3S4W}.
FT   HELIX       336    354       {ECO:0000244|PDB:3S4W}.
FT   HELIX       356    368       {ECO:0000244|PDB:3S4W}.
FT   HELIX       369    371       {ECO:0000244|PDB:3S4W}.
FT   HELIX       378    389       {ECO:0000244|PDB:3S4W}.
FT   HELIX       391    405       {ECO:0000244|PDB:3S4W}.
FT   TURN        406    408       {ECO:0000244|PDB:3S4W}.
FT   HELIX       412    426       {ECO:0000244|PDB:3S4W}.
FT   HELIX       430    441       {ECO:0000244|PDB:3S4W}.
FT   STRAND      443    445       {ECO:0000244|PDB:3S4W}.
FT   HELIX       446    461       {ECO:0000244|PDB:3S4W}.
FT   HELIX       465    481       {ECO:0000244|PDB:3S4W}.
FT   HELIX       484    500       {ECO:0000244|PDB:3S4W}.
FT   HELIX       502    507       {ECO:0000244|PDB:3S4W}.
FT   HELIX       509    513       {ECO:0000244|PDB:3S4W}.
FT   HELIX       514    521       {ECO:0000244|PDB:3S4W}.
FT   HELIX       524    541       {ECO:0000244|PDB:3S4W}.
FT   HELIX       548    561       {ECO:0000244|PDB:3S4W}.
FT   HELIX       566    582       {ECO:0000244|PDB:3S4W}.
FT   HELIX       603    619       {ECO:0000244|PDB:3S4W}.
FT   STRAND      620    622       {ECO:0000244|PDB:3S4W}.
FT   HELIX       623    639       {ECO:0000244|PDB:3S4W}.
FT   HELIX       644    662       {ECO:0000244|PDB:3S4W}.
FT   STRAND      679    681       {ECO:0000244|PDB:3S4W}.
FT   STRAND      685    687       {ECO:0000244|PDB:3S4W}.
FT   STRAND      689    692       {ECO:0000244|PDB:3S4W}.
FT   HELIX       697    706       {ECO:0000244|PDB:3S4W}.
FT   HELIX       727    742       {ECO:0000244|PDB:3S4W}.
FT   TURN        747    749       {ECO:0000244|PDB:3S4W}.
FT   HELIX       750    752       {ECO:0000244|PDB:3S4W}.
FT   STRAND      757    759       {ECO:0000244|PDB:3S4W}.
FT   STRAND      765    768       {ECO:0000244|PDB:3S4W}.
FT   HELIX       774    797       {ECO:0000244|PDB:3S4W}.
FT   HELIX       803    827       {ECO:0000244|PDB:3S4W}.
FT   HELIX       916    919       {ECO:0000244|PDB:3S4W}.
FT   TURN        920    922       {ECO:0000244|PDB:3S4W}.
FT   HELIX       928    935       {ECO:0000244|PDB:3S4W}.
FT   HELIX       960    978       {ECO:0000244|PDB:3S4W}.
FT   TURN       1001   1004       {ECO:0000244|PDB:3S4W}.
FT   HELIX      1007   1034       {ECO:0000244|PDB:3S4W}.
FT   HELIX      1050   1071       {ECO:0000244|PDB:3S4W}.
FT   TURN       1074   1077       {ECO:0000244|PDB:3S4W}.
FT   HELIX      1082   1090       {ECO:0000244|PDB:3S4W}.
FT   HELIX      1105   1117       {ECO:0000244|PDB:3S4W}.
FT   HELIX      1118   1122       {ECO:0000244|PDB:3S4W}.
FT   HELIX      1126   1140       {ECO:0000244|PDB:3S4W}.
FT   HELIX      1149   1160       {ECO:0000244|PDB:3S4W}.
FT   HELIX      1174   1190       {ECO:0000244|PDB:3S4W}.
FT   HELIX      1194   1203       {ECO:0000244|PDB:3S4W}.
FT   TURN       1204   1206       {ECO:0000244|PDB:3S4W}.
FT   HELIX      1207   1210       {ECO:0000244|PDB:3S4W}.
FT   HELIX      1226   1244       {ECO:0000244|PDB:3S4W}.
FT   HELIX      1254   1280       {ECO:0000244|PDB:3S4W}.
FT   TURN       1281   1283       {ECO:0000244|PDB:3S4W}.
FT   HELIX      1287   1305       {ECO:0000244|PDB:3S4W}.
FT   HELIX      1307   1314       {ECO:0000244|PDB:3S4W}.
FT   TURN       1315   1317       {ECO:0000244|PDB:3S4W}.
FT   HELIX      1319   1340       {ECO:0000244|PDB:3S4W}.
FT   HELIX      1344   1346       {ECO:0000244|PDB:3S4W}.
FT   HELIX      1349   1352       {ECO:0000244|PDB:3S4W}.
FT   HELIX      1355   1373       {ECO:0000244|PDB:3S4W}.
FT   HELIX      1379   1387       {ECO:0000244|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
//
DBGET integrated database retrieval system