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 03-AUG-2022, entry version 161.
DE RecName: Full=ATPase WRNIP1;
DE EC=3.6.1.- {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. Also plays 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;
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};
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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 AlphaFoldDB; Q91XU0; -.
DR SMR; Q91XU0; -.
DR BioGRID; 219695; 5.
DR IntAct; Q91XU0; 1.
DR MINT; Q91XU0; -.
DR STRING; 10090.ENSMUSP00000021832; -.
DR iPTMnet; Q91XU0; -.
DR PhosphoSitePlus; Q91XU0; -.
DR SwissPalm; Q91XU0; -.
DR EPD; Q91XU0; -.
DR jPOST; Q91XU0; -.
DR MaxQB; Q91XU0; -.
DR PaxDb; Q91XU0; -.
DR PeptideAtlas; Q91XU0; -.
DR PRIDE; Q91XU0; -.
DR ProteomicsDB; 297563; -. [Q91XU0-1]
DR ProteomicsDB; 297564; -. [Q91XU0-2]
DR Antibodypedia; 9254; 235 antibodies from 33 providers.
DR DNASU; 78903; -.
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 VEuPathDB; HostDB:ENSMUSG00000021400; -.
DR eggNOG; KOG2028; Eukaryota.
DR GeneTree; ENSGT00390000008538; -.
DR HOGENOM; CLU_017985_0_2_1; -.
DR InParanoid; Q91XU0; -.
DR OMA; ACEFVGM; -.
DR OrthoDB; 580439at2759; -.
DR PhylomeDB; Q91XU0; -.
DR TreeFam; TF324547; -.
DR BioGRID-ORCS; 78903; 1 hit in 107 CRISPR screens.
DR ChiTaRS; Wrnip1; mouse.
DR PRO; PR:Q91XU0; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q91XU0; protein.
DR Bgee; ENSMUSG00000021400; Expressed in habenula and 288 other tissues.
DR ExpressionAtlas; Q91XU0; baseline and differential.
DR Genevisible; Q91XU0; MM.
DR GO; GO:0000781; C:chromosome, telomeric region; ISO:MGI.
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:ATP hydrolysis 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:0017116; F:single-stranded DNA helicase activity; IBA:GO_Central.
DR GO; GO:0000731; P:DNA synthesis involved in DNA repair; ISS:UniProtKB.
DR GO; GO:0006261; P:DNA-templated 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-templated DNA replication initiation; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
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; IPR006642; Rad18_UBZ4.
DR InterPro; IPR040539; Znf-WRNIP1_ubi.
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 REGION 48..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..186
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 20
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 23
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 31
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q96S55"
FT BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 265..271
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96S55"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|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:0007744|PubMed:21183079"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|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
