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Database: UniProt
Entry: WRIP1_MOUSE
LinkDB: WRIP1_MOUSE
Original site: WRIP1_MOUSE 
ID   WRIP1_MOUSE             Reviewed;         660 AA.
AC   Q91XU0; Q3TCT7; Q6PDF0; Q8BUW5; Q8BWP6; Q8BY55; Q921W3; Q9EQL3;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 2.
DT   11-DEC-2019, entry version 150.
DE   RecName: Full=ATPase WRNIP1;
DE            EC=3.6.1.3 {ECO:0000250|UniProtKB:Q96S55};
DE   AltName: Full=Werner helicase-interacting protein 1;
GN   Name=Wrnip1 {ECO:0000312|MGI:MGI:1926153}; Synonyms=Whip;
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] {ECO:0000305, ECO:0000312|EMBL:BAB60708.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH WRN, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB60708.1};
RC   TISSUE=Testis {ECO:0000312|EMBL:BAB60708.1};
RX   PubMed=11301316; DOI=10.1074/jbc.c100035200;
RA   Kawabe Y., Branzei D., Hayashi T., Suzuki H., Masuko T., Onoda F.,
RA   Heo S.-J., Ikeda H., Shimamoto A., Furuichi Y., Seki M., Enomoto T.;
RT   "A novel protein interacts with the Werner's syndrome gene product
RT   physically and functionally.";
RL   J. Biol. Chem. 276:20364-20369(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Cerebellum, Liver, Placenta, and Thymus;
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   [3]
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   [4] {ECO:0000305, ECO:0000312|EMBL:AAH10482.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=Czech II {ECO:0000312|EMBL:AAH10482.1}, and
RC   FVB/N-3 {ECO:0000312|EMBL:AAH58744.1};
RC   TISSUE=Mammary gland {ECO:0000312|EMBL:AAH10482.1};
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] {ECO:0000305, ECO:0000312|EMBL:CAI25647.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 182-660 (ISOFORM 1).
RA   Shannon M., Ramirez M., Thelen M.P.;
RT   "Characterization of RuvB homologs in human and mouse.";
RL   Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-91 AND SER-92, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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).
CC   -!- FUNCTION: Functions as a modulator of initiation or reinitiation events
CC       during DNA polymerase delta-mediated DNA synthesis. In the presence of
CC       ATP, stimulation of DNA polymerase delta-mediated DNA synthesis is
CC       decreased. Plays also a role in the innate immune defense against
CC       viruses. Stabilizes the RIG-I/DDX58 dsRNA interaction and promotes RIG-
CC       I/DDX58 'Lys-63'-linked polyubiquitination. In turn, RIG-I/DDX58
CC       transmits the signal through mitochondrial MAVS.
CC       {ECO:0000250|UniProtKB:Q96S55}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.1.3;
CC         Evidence={ECO:0000250|UniProtKB:Q96S55};
CC   -!- SUBUNIT: Forms homooligomers, possibly octamers. Directly interacts
CC       with POLD1, POLD2 and POLD4 (By similarity). Interacts with the N-
CC       terminal domain of WRN (By similarity). Interacts (via UBZ4-type zinc
CC       finger) with monoubiquitin and polyubiquitin. Interacts with TRIM14 and
CC       PPP6C; these interactions positively regulate the RIG-I/DDX58 signaling
CC       pathway (By similarity). {ECO:0000250|UniProtKB:Q96S55,
CC       ECO:0000269|PubMed:11301316}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11301316}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q96S55}. Note=Colocalizes with WRN in granular
CC       structures in the nucleus. {ECO:0000269|PubMed:11301316}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1 {ECO:0000269|PubMed:11301316};
CC         IsoId=Q91XU0-1; Sequence=Displayed;
CC       Name=2 {ECO:0000305};
CC         IsoId=Q91XU0-2; Sequence=VSP_051784, VSP_051785;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC       {ECO:0000250|UniProtKB:Q96S55}.
CC   -!- DOMAIN: The UBZ4-type zinc finger binds ubiquitin.
CC       {ECO:0000250|UniProtKB:Q96S55}.
CC   -!- PTM: Sumoylated with SUMO1 and SUMO2/3. {ECO:0000250|UniProtKB:Q96S55}.
CC   -!- MISCELLANEOUS: [Isoform 2]: Due to intron retention. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. RarA/MGS1/WRNIP1
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG35725.1; Type=Frameshift; Evidence={ECO:0000305};
DR   EMBL; AB056151; BAB60708.1; -; mRNA.
DR   EMBL; AK041886; BAC31091.1; -; mRNA.
DR   EMBL; AK050368; BAC34213.1; -; mRNA.
DR   EMBL; AK082078; BAC38404.1; -; mRNA.
DR   EMBL; AK167570; BAE39633.1; -; mRNA.
DR   EMBL; AK170542; BAE41868.1; -; mRNA.
DR   EMBL; AK170846; BAE42069.1; -; mRNA.
DR   EMBL; AL645808; CAI25647.1; -; Genomic_DNA.
DR   EMBL; BC010482; AAH10482.1; -; mRNA.
DR   EMBL; BC058744; AAH58744.1; -; mRNA.
DR   EMBL; AF208046; AAG35725.1; ALT_FRAME; mRNA.
DR   CCDS; CCDS26427.1; -. [Q91XU0-1]
DR   RefSeq; NP_084491.3; NM_030215.3. [Q91XU0-1]
DR   SMR; Q91XU0; -.
DR   BioGrid; 219695; 3.
DR   IntAct; Q91XU0; 2.
DR   MINT; Q91XU0; -.
DR   STRING; 10090.ENSMUSP00000021832; -.
DR   iPTMnet; Q91XU0; -.
DR   PhosphoSitePlus; Q91XU0; -.
DR   SwissPalm; Q91XU0; -.
DR   EPD; Q91XU0; -.
DR   jPOST; Q91XU0; -.
DR   PaxDb; Q91XU0; -.
DR   PeptideAtlas; Q91XU0; -.
DR   PRIDE; Q91XU0; -.
DR   Ensembl; ENSMUST00000021832; ENSMUSP00000021832; ENSMUSG00000021400. [Q91XU0-1]
DR   GeneID; 78903; -.
DR   KEGG; mmu:78903; -.
DR   UCSC; uc007pzs.2; mouse. [Q91XU0-2]
DR   UCSC; uc007pzt.2; mouse. [Q91XU0-1]
DR   CTD; 56897; -.
DR   MGI; MGI:1926153; Wrnip1.
DR   eggNOG; KOG2028; Eukaryota.
DR   eggNOG; COG2256; LUCA.
DR   GeneTree; ENSGT00390000008538; -.
DR   InParanoid; Q91XU0; -.
DR   KO; K07478; -.
DR   OMA; RIILSQC; -.
DR   OrthoDB; 580439at2759; -.
DR   PhylomeDB; Q91XU0; -.
DR   TreeFam; TF324547; -.
DR   ChiTaRS; Wrnip1; mouse.
DR   PRO; PR:Q91XU0; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; Q91XU0; protein.
DR   Bgee; ENSMUSG00000021400; Expressed in 305 organ(s), highest expression level in supraoptic nucleus.
DR   ExpressionAtlas; Q91XU0; baseline and differential.
DR   Genevisible; Q91XU0; MM.
DR   GO; GO:0000784; C:nuclear chromosome, telomeric region; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008047; F:enzyme activator activity; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000731; P:DNA synthesis involved in DNA repair; ISS:UniProtKB.
DR   GO; GO:0006261; P:DNA-dependent DNA replication; IBA:GO_Central.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0006282; P:regulation of DNA repair; IBA:GO_Central.
DR   GO; GO:0030174; P:regulation of DNA-dependent DNA replication initiation; ISS:UniProtKB.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR032423; AAA_assoc_2.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR   InterPro; IPR021886; MgsA_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR040539; Znf-WRNIP1_ubi.
DR   InterPro; IPR006642; Znf_Rad18_put.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF16193; AAA_assoc_2; 1.
DR   Pfam; PF12002; MgsA_C; 1.
DR   Pfam; PF18279; zf-WRNIP1_ubi; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00734; ZnF_Rad18; 1.
DR   SUPFAM; SSF48019; SSF48019; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51908; ZF_UBZ4; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; Cytoplasm; DNA damage;
KW   DNA repair; DNA replication; Hydrolase; Immunity; Innate immunity;
KW   Isopeptide bond; Metal-binding; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..660
FT                   /note="ATPase WRNIP1"
FT                   /id="PRO_0000084786"
FT   ZN_FING         17..44
FT                   /note="UBZ4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT   NP_BIND         265..271
FT                   /note="ATP"
FT                   /evidence="ECO:0000250|UniProtKB:P55072"
FT   COMPBIAS        144..210
FT                   /note="Ala-rich"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00001"
FT   METAL           20
FT                   /note="Zinc"
FT                   /evidence="ECO:0000250|UniProtKB:Q96S55"
FT   METAL           23
FT                   /note="Zinc"
FT                   /evidence="ECO:0000250|UniProtKB:Q96S55"
FT   METAL           31
FT                   /note="Zinc; via tele nitrogen"
FT                   /evidence="ECO:0000250|UniProtKB:Q96S55"
FT   METAL           35
FT                   /note="Zinc; via tele nitrogen"
FT                   /evidence="ECO:0000250|UniProtKB:Q96S55"
FT   METAL           39
FT                   /note="Zinc"
FT                   /evidence="ECO:0000250|UniProtKB:Q96S55"
FT   MOD_RES         65
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96S55"
FT   MOD_RES         75
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:21183079"
FT   MOD_RES         85
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96S55"
FT   MOD_RES         91
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:21183079"
FT   MOD_RES         92
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:17242355,
FT                   ECO:0000244|PubMed:21183079"
FT   MOD_RES         116
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96S55"
FT   MOD_RES         153
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96S55"
FT   MOD_RES         529
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96S55"
FT   MOD_RES         557
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96S55"
FT   MOD_RES         628
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q96S55"
FT   CROSSLNK        81
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96S55"
FT   CROSSLNK        141
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96S55"
FT   CROSSLNK        220
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96S55"
FT   CROSSLNK        296
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96S55"
FT   CROSSLNK        305
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96S55"
FT   CROSSLNK        311
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96S55"
FT   CROSSLNK        317
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96S55"
FT   CROSSLNK        330
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96S55"
FT   CROSSLNK        477
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q96S55"
FT   CROSSLNK        477
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q96S55"
FT   CROSSLNK        622
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96S55"
FT   CROSSLNK        628
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q96S55"
FT   CROSSLNK        631
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96S55"
FT   VAR_SEQ         544..568
FT                   /note="LADPSALAQAVAAYQGCHFIGMPEC -> EWRRVCVGVGVLRGGVLTLVWSH
FT                   AE (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_051784"
FT   VAR_SEQ         569..660
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_051785"
FT   CONFLICT        180
FT                   /note="G -> V (in Ref. 2; BAC34213)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        202..203
FT                   /note="RA -> P (in Ref. 5; AAG35725)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        232
FT                   /note="Q -> H (in Ref. 5; AAG35725)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        243
FT                   /note="Q -> E (in Ref. 1; BAB60708)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        453
FT                   /note="R -> K (in Ref. 1; BAB60708)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        455
FT                   /note="V -> M (in Ref. 4; AAH10482)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        499
FT                   /note="S -> C (in Ref. 2; BAC38404)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        566
FT                   /note="P -> H (in Ref. 1; BAB60708)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   660 AA;  71794 MW;  A9114A131B5F9763 CRC64;
     MEVSGPEDDP FLSQLHQVQC PVCQQMMPAA HINSHLDRCL LLHPAGHAEP AAGSHRAGER
     AKGPSPPGAK RRRLSESSAL KQPATPTAAE SSEGEGEEGD DGGETESRES YDAPPTPSGA
     RLIPDFPVAR SSSPARKGMG KRPAAAAAAG SASPRSWDEA EAQEEEEAGV DGDGDADVDG
     EDDPGHWDAD AADASFGVSA GRAHPRALAA EEIRQMLEGK PLADKMRPDT LQDYIGQSRA
     VGQETLLRSL LEANEIPSLI LWGPPGCGKT TLAHIIANNS KKHSIRFVTL SATNAKTNDV
     RDVIKQAQNE KSFFKRKTIL FIDEIHRFNK SQQDTFLPHV ECGTITLIGA TTENPSFQVN
     AALLSRCRVI VLEKLPVEAM VTILMRAINS LGIHVLDSSR PTDPLSHSSN CSSEPSVFIE
     DKAVDTLAYL SDGDARTGLN GLQLAVLARL SSRKVFCKKS GQTYSPSRVL ITENDVKEGL
     QRSHILYDRA GEEHYNCISA LHKAMRGSDQ NASLYWLARM LEGGEDPLYV ARRLVRFASE
     DIGLADPSAL AQAVAAYQGC HFIGMPECEV LLAQCVVYFA RAPKSIEVYS AYNNVKACLR
     SHQGPLPPVP LHLRNAPTRL MKDLGYGKGY KYNPMYSEPV DQDYLPEELR GVDFFKQRRC
//
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