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 24-JAN-2024, entry version 169. 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; RC 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 FVB/N-3 RC {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 RIGI dsRNA interaction and promotes RIGI 'Lys- CC 63'-linked polyubiquitination. In turn, RIGI transmits the signal CC through mitochondrial MAVS. {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 RIGI 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 7. 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 MaxQB; Q91XU0; -. DR PaxDb; 10090-ENSMUSP00000021832; -. DR PeptideAtlas; Q91XU0; -. DR ProteomicsDB; 297563; -. [Q91XU0-1] DR ProteomicsDB; 297564; -. [Q91XU0-2] DR Pumba; Q91XU0; -. DR Antibodypedia; 9254; 250 antibodies from 33 providers. DR DNASU; 78903; -. DR Ensembl; ENSMUST00000021832.7; ENSMUSP00000021832.7; ENSMUSG00000021400.9. [Q91XU0-1] DR GeneID; 78903; -. DR KEGG; mmu:78903; -. DR UCSC; uc007pzs.2; mouse. [Q91XU0-2] DR UCSC; uc007pzt.2; mouse. [Q91XU0-1] DR AGR; MGI:1926153; -. 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; RIILSQC; -. DR OrthoDB; 206891at2759; -. DR PhylomeDB; Q91XU0; -. DR TreeFam; TF324547; -. DR BioGRID-ORCS; 78903; 2 hits in 112 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 292 other cell types or tissues. DR ExpressionAtlas; Q91XU0; baseline and differential. DR GO; GO:0000781; C: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: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:0030174; P:regulation of DNA-templated DNA replication initiation; ISS:UniProtKB. DR CDD; cd00009; AAA; 1. DR CDD; cd18139; HLD_clamp_RarA; 1. DR Gene3D; 1.10.8.60; -; 1. DR Gene3D; 1.20.272.10; -; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1. DR Gene3D; 1.10.3710.10; DNA polymerase III clamp loader subunits, C-terminal domain; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 PANTHER; PTHR13779:SF7; ATPASE WRNIP1; 1. DR PANTHER; PTHR13779; WERNER HELICASE-INTERACTING PROTEIN 1 FAMILY MEMBER; 1. 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1. DR PROSITE; PS51908; ZF_UBZ4; 1. DR Genevisible; Q91XU0; MM. 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 //