ID RUFY3_HUMAN Reviewed; 469 AA. AC Q7L099; B3KM25; B4DYW7; D9N163; O94948; Q9UI00; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 24-JAN-2024, entry version 147. DE RecName: Full=Protein RUFY3 {ECO:0000305}; DE AltName: Full=RUN and FYVE domain-containing protein 3 {ECO:0000312|HGNC:HGNC:30285}; DE AltName: Full=Rap2-interacting protein x {ECO:0000250|UniProtKB:Q9D394}; DE Short=RIPx {ECO:0000250|UniProtKB:Q9D394}; DE AltName: Full=Single axon-regulated protein {ECO:0000250|UniProtKB:Q5FVJ0}; DE Short=Singar {ECO:0000250|UniProtKB:Q5FVJ0}; GN Name=RUFY3 {ECO:0000312|HGNC:HGNC:30285}; Synonyms=KIAA0871; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=10048485; DOI=10.1093/dnares/5.6.355; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 5:355-364(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4). RC TISSUE=Embryo, and Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; 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] RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Adrenal gland; RA Peng Y., Gu Y., Gu J., Huang Q., Fu S., Wu T., Dong H., Jin W., Fu G., RA Han Z., Chen Z., Wang Y.; RT "A novel gene expressed in human adrenal gland."; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [6] RP INTERACTION WITH RAS-RELATED PROTEINS, AND SUBCELLULAR LOCATION. RX PubMed=20376209; DOI=10.7150/ijbs.6.187; RA Yoshida H., Okumura N., Kitagishi Y., Shirafuji N., Matsuda S.; RT "Rab5(Q79L) interacts with the carboxyl terminus of RUFY3."; RL Int. J. Biol. Sci. 6:187-189(2010). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [8] RP FUNCTION, INTERACTION WITH PAK1, PHOSPHORYLATION, SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. RX PubMed=25766321; DOI=10.1038/cddis.2015.50; RA Wang G., Zhang Q., Song Y., Wang X., Guo Q., Zhang J., Li J., Han Y., RA Miao Z., Li F.; RT "PAK1 regulates RUFY3-mediated gastric cancer cell migration and RT invasion."; RL Cell Death Dis. 6:E1682-E1682(2015). CC -!- FUNCTION: Plays a role in the generation of neuronal polarity formation CC and axon growth (By similarity). Implicated in the formation of a CC single axon by developing neurons (By similarity). May inhibit the CC formation of additional axons by inhibition of PI3K in minor neuronal CC processes (By similarity). Plays a role in the formation of F-actin- CC enriched protrusive structures at the cell periphery (PubMed:25766321). CC Plays a role in cytoskeletal organization by regulating the subcellular CC localization of FSCN1 and DBN1 at axonal growth cones (By similarity). CC Promotes gastric cancer cell migration and invasion in a PAK1-dependent CC manner (PubMed:25766321). {ECO:0000250|UniProtKB:Q5FVJ0, CC ECO:0000250|UniProtKB:Q9D394, ECO:0000269|PubMed:25766321}. CC -!- SUBUNIT: Interacts with PAK1 (PubMed:25766321). Interacts (via C- CC terminus) with Ras-related Rab-5 proteins (PubMed:20376209). Interacts CC (via C-terminus) with Ras-related Rap-2 proteins (PubMed:20376209). CC Interacts with PIK3CA and PIK3R1 (By similarity). Interacts (via N- CC terminus) with FSCN1; this interaction induces neuron axon development CC (By similarity). Interacts with DBN1 (By similarity). CC {ECO:0000250|UniProtKB:Q5FVJ0, ECO:0000250|UniProtKB:Q9D394, CC ECO:0000269|PubMed:20376209, ECO:0000269|PubMed:25766321}. CC -!- INTERACTION: CC Q7L099; Q9P2A4: ABI3; NbExp=3; IntAct=EBI-722392, EBI-742038; CC Q7L099; P20807-4: CAPN3; NbExp=3; IntAct=EBI-722392, EBI-11532021; CC Q7L099; Q14088: RAB33A; NbExp=5; IntAct=EBI-722392, EBI-744685; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25766321}. CC Endomembrane system {ECO:0000269|PubMed:20376209}. Cell projection, CC invadopodium {ECO:0000269|PubMed:25766321}. Perikaryon CC {ECO:0000250|UniProtKB:Q9D394}. Cell projection CC {ECO:0000250|UniProtKB:Q9D394}. Cell projection, growth cone CC {ECO:0000250|UniProtKB:Q9D394}. Cell projection, filopodium CC {ECO:0000250|UniProtKB:Q9D394}. Cell projection, lamellipodium CC {ECO:0000250|UniProtKB:Q9D394}. Note=Colocalizes with PAK1, F-actin, CC myosins and integrins in invadopodia at the cell periphery CC (PubMed:25766321). Colocalized with Ras-related Rab-5 proteins in CC cytoplasmic vesicles (PubMed:20376209). Accumulates in axon growth CC cones in a F-actin-dependent manner (By similarity). Colocalized with CC FSCN1 and F-actin at filipodia and lamellipodia of axonal growth cones CC (By similarity). Colocalized with DBN1 and F-actin at transitional CC domain of the axonal growth cone (By similarity). CC {ECO:0000250|UniProtKB:Q5FVJ0, ECO:0000250|UniProtKB:Q9D394, CC ECO:0000269|PubMed:20376209, ECO:0000269|PubMed:25766321}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q7L099-1; Sequence=Displayed; CC Name=2; CC IsoId=Q7L099-2; Sequence=VSP_041250, VSP_041254, VSP_041255; CC Name=3; CC IsoId=Q7L099-3; Sequence=VSP_041253; CC Name=4; CC IsoId=Q7L099-4; Sequence=VSP_041251, VSP_041252, VSP_041253; CC -!- TISSUE SPECIFICITY: Overexpressed in gastric cancer cells and tissues CC (at protein level) (PubMed:25766321). {ECO:0000269|PubMed:25766321}. CC -!- PTM: Phosphorylated by PAK1 (PubMed:25766321). Isoform 1 is partially CC phosphorylated (By similarity). {ECO:0000250|UniProtKB:Q5FVJ0, CC ECO:0000269|PubMed:25766321}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA74894.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAF17208.1; 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; AB020678; BAA74894.2; ALT_INIT; mRNA. DR EMBL; AK000911; BAG50837.1; -; mRNA. DR EMBL; AK302637; BAG63879.1; -; mRNA. DR EMBL; AC009570; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC051716; AAH51716.1; -; mRNA. DR EMBL; AF112221; AAF17208.1; ALT_FRAME; mRNA. DR CCDS; CCDS34001.1; -. [Q7L099-3] DR CCDS; CCDS3547.1; -. [Q7L099-1] DR CCDS; CCDS47068.1; -. [Q7L099-2] DR CCDS; CCDS75138.1; -. [Q7L099-4] DR RefSeq; NP_001032519.1; NM_001037442.3. [Q7L099-3] DR RefSeq; NP_001124181.1; NM_001130709.1. [Q7L099-2] DR RefSeq; NP_001278922.1; NM_001291993.1. [Q7L099-4] DR RefSeq; NP_001278923.1; NM_001291994.1. DR RefSeq; NP_001332769.1; NM_001345840.1. DR RefSeq; NP_055776.1; NM_014961.4. [Q7L099-1] DR AlphaFoldDB; Q7L099; -. DR SMR; Q7L099; -. DR BioGRID; 116566; 45. DR IntAct; Q7L099; 25. DR MINT; Q7L099; -. DR STRING; 9606.ENSP00000370394; -. DR GlyGen; Q7L099; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q7L099; -. DR PhosphoSitePlus; Q7L099; -. DR BioMuta; RUFY3; -. DR DMDM; 74738521; -. DR EPD; Q7L099; -. DR jPOST; Q7L099; -. DR MassIVE; Q7L099; -. DR MaxQB; Q7L099; -. DR PaxDb; 9606-ENSP00000370394; -. DR PeptideAtlas; Q7L099; -. DR ProteomicsDB; 68727; -. [Q7L099-1] DR ProteomicsDB; 68728; -. [Q7L099-2] DR ProteomicsDB; 68729; -. [Q7L099-3] DR ProteomicsDB; 68730; -. [Q7L099-4] DR Pumba; Q7L099; -. DR ABCD; Q7L099; 3 sequenced antibodies. DR Antibodypedia; 12878; 76 antibodies from 23 providers. DR DNASU; 22902; -. DR Ensembl; ENST00000226328.8; ENSP00000226328.4; ENSG00000018189.13. [Q7L099-1] DR Ensembl; ENST00000381006.8; ENSP00000370394.3; ENSG00000018189.13. [Q7L099-3] DR Ensembl; ENST00000417478.6; ENSP00000399771.2; ENSG00000018189.13. [Q7L099-2] DR Ensembl; ENST00000502653.5; ENSP00000425400.1; ENSG00000018189.13. [Q7L099-4] DR GeneID; 22902; -. DR KEGG; hsa:22902; -. DR MANE-Select; ENST00000381006.8; ENSP00000370394.3; NM_001037442.4; NP_001032519.1. [Q7L099-3] DR UCSC; uc003hfp.5; human. [Q7L099-1] DR AGR; HGNC:30285; -. DR CTD; 22902; -. DR DisGeNET; 22902; -. DR GeneCards; RUFY3; -. DR HGNC; HGNC:30285; RUFY3. DR HPA; ENSG00000018189; Tissue enhanced (retina). DR MIM; 611194; gene. DR neXtProt; NX_Q7L099; -. DR OpenTargets; ENSG00000018189; -. DR PharmGKB; PA142670961; -. DR VEuPathDB; HostDB:ENSG00000018189; -. DR eggNOG; KOG4381; Eukaryota. DR GeneTree; ENSGT00940000156035; -. DR HOGENOM; CLU_014576_0_0_1; -. DR InParanoid; Q7L099; -. DR OMA; XATVNNL; -. DR OrthoDB; 5385125at2759; -. DR PhylomeDB; Q7L099; -. DR TreeFam; TF323904; -. DR PathwayCommons; Q7L099; -. DR SignaLink; Q7L099; -. DR BioGRID-ORCS; 22902; 7 hits in 1154 CRISPR screens. DR ChiTaRS; RUFY3; human. DR GenomeRNAi; 22902; -. DR Pharos; Q7L099; Tbio. DR PRO; PR:Q7L099; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; Q7L099; Protein. DR Bgee; ENSG00000018189; Expressed in substantia nigra pars compacta and 203 other cell types or tissues. DR ExpressionAtlas; Q7L099; baseline and differential. DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW. DR GO; GO:0030424; C:axon; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0030425; C:dendrite; ISS:UniProtKB. DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell. DR GO; GO:0030175; C:filopodium; ISS:HGNC-UCL. DR GO; GO:0030426; C:growth cone; ISS:UniProtKB. DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0043025; C:neuronal cell body; IBA:GO_Central. DR GO; GO:0043204; C:perikaryon; ISS:UniProtKB. DR GO; GO:0007015; P:actin filament organization; ISS:UniProtKB. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0050771; P:negative regulation of axonogenesis; ISS:HGNC-UCL. DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW. DR GO; GO:0045773; P:positive regulation of axon extension; ISS:UniProtKB. DR GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB. DR GO; GO:0090316; P:positive regulation of intracellular protein transport; ISS:UniProtKB. DR GO; GO:0050770; P:regulation of axonogenesis; IBA:GO_Central. DR GO; GO:2000114; P:regulation of establishment of cell polarity; ISS:UniProtKB. DR CDD; cd17696; RUN_RUFY3; 1. DR Gene3D; 1.20.5.170; -; 1. DR Gene3D; 1.20.58.900; -; 1. DR InterPro; IPR047335; RUFY1-3. DR InterPro; IPR004012; Run_dom. DR InterPro; IPR037213; Run_dom_sf. DR InterPro; IPR047334; RUN_RUFY3. DR PANTHER; PTHR45956:SF1; PROTEIN RUFY3; 1. DR PANTHER; PTHR45956; RUN AND FYVE DOMAIN-CONTAINING PROTEIN 2-LIKE PROTEIN; 1. DR Pfam; PF02759; RUN; 1. DR SMART; SM00593; RUN; 1. DR SUPFAM; SSF140741; RUN domain-like; 1. DR PROSITE; PS50826; RUN; 1. DR Genevisible; Q7L099; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cell junction; Cell projection; Coiled coil; KW Cytoplasm; Developmental protein; Differentiation; Membrane; Neurogenesis; KW Oncogene; Phosphoprotein; Reference proteome. FT CHAIN 1..469 FT /note="Protein RUFY3" FT /id="PRO_0000245833" FT DOMAIN 95..227 FT /note="RUN" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00178" FT COILED 267..464 FT /evidence="ECO:0000255" FT MOD_RES 5 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q5FVJ0" FT MOD_RES 12 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q5FVJ0" FT MOD_RES 34 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9D394" FT MOD_RES 49 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9D394" FT MOD_RES 51 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9D394" FT VAR_SEQ 1..60 FT /note="MSALTPPTDMPTPTTDKITQAAMETIYLCKFRVSMDGEWLCLRELDDISLTP FT DPEPTHED -> MAETPPPPTAGAESCSEEPARGGEWRPEEPRRAPAGGTDREGEAGPP FT PASPAGQSEPDSPVAAPFFLLYPGDGGAGFGVRPPPQQQRSWRTPPSPGSPLPFLLLSY FT PSGGGGSSGSGKHH (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_041250" FT VAR_SEQ 1..53 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_041251" FT VAR_SEQ 54..58 FT /note="PEPTH -> MRDDT (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_041252" FT VAR_SEQ 446..469 FT /note="SEKDLVKQAKTLNSAANKLIPKHH -> RLRQAERSRQSAELDNRLFKQDFG FT DKINSLQLEVEELTRQRNQLELELKQEKERRLQNDRSIPGRGSQKSESKMDGKHKMQEE FT NVKLKKPLEESHRLQPHPMDEQDQLLLSEKPQLCQLCQEDGSLTKNVCKNCSGTFCDAC FT STNELPLPSSIKLERVCNPCHKHLMKQYSTSPS (in isoform 3 and isoform FT 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_041253" FT VAR_SEQ 446 FT /note="S -> R (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_041254" FT VAR_SEQ 447..469 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_041255" FT CONFLICT 151 FT /note="K -> R (in Ref. 5; AAF17208)" FT /evidence="ECO:0000305" FT CONFLICT 357 FT /note="L -> S (in Ref. 2; BAG63879)" FT /evidence="ECO:0000305" FT CONFLICT Q7L099-4:304 FT /note="L -> S (in Ref. 2; BAG63879)" FT /evidence="ECO:0000305" FT CONFLICT Q7L099-4:431 FT /note="R -> G (in Ref. 2; BAG63879)" FT /evidence="ECO:0000305" SQ SEQUENCE 469 AA; 52965 MW; E8657DF068BE4113 CRC64; MSALTPPTDM PTPTTDKITQ AAMETIYLCK FRVSMDGEWL CLRELDDISL TPDPEPTHED PNYLMANERM NLMNMAKLSI KGLIESALNL GRTLDSDYAP LQQFFVVMEH CLKHGLKAKK TFLGQNKSFW GPLELVEKLV PEAAEITASV KDLPGLKTPV GRGRAWLRLA LMQKKLSEYM KALINKKELL SEFYEPNALM MEEEGAIIAG LLVGLNVIDA NFCMKGEDLD SQVGVIDFSM YLKDGNSSKG TEGDGQITAI LDQKNYVEEL NRHLNATVNN LQAKVDALEK SNTKLTEELA VANNRIITLQ EEMERVKEES SYILESNRKG PKQDRTAEGQ ALSEARKHLK EETQLRLDVE KELEMQISMR QEMELAMKML EKDVCEKQDA LVSLRQQLDD LRALKHELAF KLQSSDLGVK QKSELNSRLE EKTNQMAATI KQLEQSEKDL VKQAKTLNSA ANKLIPKHH //