RUFY3_HUMAN
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 03-AUG-2022, entry version 139.
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 CAUTION: [Isoform 2]:
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; 39.
DR IntAct; Q7L099; 21.
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; Q7L099; -.
DR PeptideAtlas; Q7L099; -.
DR PRIDE; Q7L099; -.
DR ProteomicsDB; 68727; -. [Q7L099-1]
DR ProteomicsDB; 68728; -. [Q7L099-2]
DR ProteomicsDB; 68729; -. [Q7L099-3]
DR ProteomicsDB; 68730; -. [Q7L099-4]
DR ABCD; Q7L099; 3 sequenced antibodies.
DR Antibodypedia; 12878; 73 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 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; LDESHRC; -.
DR OrthoDB; 753155at2759; -.
DR PhylomeDB; Q7L099; -.
DR TreeFam; TF323904; -.
DR PathwayCommons; Q7L099; -.
DR SignaLink; Q7L099; -.
DR BioGRID-ORCS; 22902; 7 hits in 1078 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 201 other tissues.
DR ExpressionAtlas; Q7L099; baseline and differential.
DR Genevisible; Q7L099; HS.
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 Gene3D; 1.20.58.900; -; 1.
DR InterPro; IPR004012; Run_dom.
DR InterPro; IPR037213; Run_dom_sf.
DR Pfam; PF02759; RUN; 1.
DR SMART; SM00593; RUN; 1.
DR SUPFAM; SSF140741; SSF140741; 1.
DR PROSITE; PS50826; RUN; 1.
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
