RBNS5_HUMAN
ID RBNS5_HUMAN Reviewed; 784 AA.
AC Q9H1K0; B4DWY8; C9J4P5; Q3KP30; Q59EY8; Q8NAQ1;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Rabenosyn-5 {ECO:0000303|PubMed:11062261};
DE AltName: Full=110 kDa protein;
DE AltName: Full=FYVE finger-containing Rab5 effector protein rabenosyn-5;
DE AltName: Full=RAB effector RBSN {ECO:0000312|HGNC:HGNC:20759};
DE AltName: Full=Zinc finger FYVE domain-containing protein 20;
GN Name=RBSN {ECO:0000312|HGNC:HGNC:20759};
GN Synonyms=ZFYVE20 {ECO:0000312|HGNC:HGNC:20759};
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 [MRNA] (ISOFORM 1), FUNCTION IN ENDOSOMAL RECYCLING,
RP INTERACTION WITH PTDINSP3; GTP-BOUND RAB5A AND VPS45A, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Cervix carcinoma;
RX PubMed=11062261; DOI=10.1083/jcb.151.3.601;
RA Nielsen E., Christoforidis S., Uttenweiler-Joseph S., Miaczynska M.,
RA Dewitte F., Wilm M., Hoflack B., Zerial M.;
RT "Rabenosyn-5, a novel Rab5 effector, is complexed with hVPS45 and recruited
RT to endosomes through a FYVE finger domain.";
RL J. Cell Biol. 151:601-612(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 501-784 (ISOFORM 1).
RC TISSUE=Brain, 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=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-755 (ISOFORM 1).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION IN ENDOSOMAL RECYCLING, INTERACTION WITH RAB4A AND RAB5A, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11788822; DOI=10.1038/ncb744;
RA de Renzis S., Soennichsen B., Zerial M.;
RT "Divalent Rab effectors regulate the sub-compartmental organization and
RT sorting of early endosomes.";
RL Nat. Cell Biol. 4:124-133(2002).
RN [7]
RP FUNCTION IN ENDOSOMAL RECYCLING, INTERACTION WITH EHD1, MUTAGENESIS OF
RP 626-ASN--PHE-628 AND 662-ASN--PHE-664, AND SUBCELLULAR LOCATION.
RX PubMed=15020713; DOI=10.1091/mbc.e03-10-0733;
RA Naslavsky N., Boehm M., Backlund P.S. Jr., Caplan S.;
RT "Rabenosyn-5 and EHD1 interact and sequentially regulate protein recycling
RT to the plasma membrane.";
RL Mol. Biol. Cell 15:2410-2422(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [9]
RP INTERACTION WITH RAB4A.
RX PubMed=20098723; DOI=10.1371/journal.pbio.1000283;
RA Hoogenraad C.C., Popa I., Futai K., Martinez-Sanchez E.,
RA Sanchez-Martinez E., Wulf P.S., van Vlijmen T., Dortland B.R., Oorschot V.,
RA Govers R., Monti M., Heck A.J., Sheng M., Klumperman J., Rehmann H.,
RA Jaarsma D., Kapitein L.C., van der Sluijs P.;
RT "Neuron specific Rab4 effector GRASP-1 coordinates membrane specialization
RT and maturation of recycling endosomes.";
RL PLoS Biol. 8:E1000283-E1000283(2010).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22308388; DOI=10.1073/pnas.1115495109;
RA Navaroli D.M., Bellve K.D., Standley C., Lifshitz L.M., Cardia J.,
RA Lambright D., Leonard D., Fogarty K.E., Corvera S.;
RT "Rabenosyn-5 defines the fate of the transferrin receptor following
RT clathrin-mediated endocytosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:E471-E480(2012).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-219; SER-226 AND
RP SER-230, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-684, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) OF 458-503 AND 728-784 IN COMPLEX
RP WITH RAB22A, AND INTERACTION WITH RAB4A; RAB5A; RAB14; RAB22A AND RAB24.
RX PubMed=16034420; DOI=10.1038/nature03798;
RA Eathiraj S., Pan X., Ritacco C., Lambright D.G.;
RT "Structural basis of family-wide Rab GTPase recognition by rabenosyn-5.";
RL Nature 436:415-419(2005).
RN [15]
RP VARIANT ARG-425.
RX PubMed=25233840; DOI=10.1186/s13023-014-0141-5;
RA Stockler S., Corvera S., Lambright D., Fogarty K., Nosova E., Leonard D.,
RA Steinfeld R., Ackerley C., Shyr C., Au N., Selby K., van Allen M.,
RA Vallance H., Wevers R., Watkins D., Rosenblatt D., Ross C.J., Conibear E.,
RA Wasserman W., van Karnebeek C.;
RT "Single point mutation in Rabenosyn-5 in a female with intractable seizures
RT and evidence of defective endocytotic trafficking.";
RL Orphanet J. Rare Dis. 9:141-141(2014).
CC -!- FUNCTION: Rab4/Rab5 effector protein acting in early endocytic membrane
CC fusion and membrane trafficking of recycling endosomes. Required for
CC endosome fusion either homotypically or with clathrin coated vesicles.
CC Plays a role in the lysosomal trafficking of CTSD/cathepsin D from the
CC Golgi to lysosomes. Also promotes the recycling of transferrin directly
CC from early endosomes to the plasma membrane. Binds phospholipid
CC vesicles containing phosphatidylinositol 3-phosphate (PtdInsP3)
CC (PubMed:11062261, PubMed:11788822, PubMed:15020713). Plays a role in
CC the recycling of transferrin receptor to the plasma membrane
CC (PubMed:22308388). {ECO:0000269|PubMed:11062261,
CC ECO:0000269|PubMed:11788822, ECO:0000269|PubMed:15020713,
CC ECO:0000269|PubMed:22308388}.
CC -!- SUBUNIT: Interacts with EHD1, RAB4A, RAB5A, RAB14, RAB22A, RAB24 and
CC VPS45 (PubMed:11062261, PubMed:15020713, PubMed:16034420). Binds
CC simultaneously to RAB4A and RAB5A in vitro (PubMed:16034420). Interacts
CC with RAB4A and RAB5A that has been activated by GTP binding
CC (PubMed:11062261, PubMed:16034420, PubMed:20098723, PubMed:11788822).
CC {ECO:0000269|PubMed:11062261, ECO:0000269|PubMed:11788822,
CC ECO:0000269|PubMed:15020713, ECO:0000269|PubMed:16034420,
CC ECO:0000269|PubMed:20098723}.
CC -!- INTERACTION:
CC Q9H1K0; Q9H4M9: EHD1; NbExp=4; IntAct=EBI-1105310, EBI-490691;
CC Q9H1K0; P20338: RAB4A; NbExp=4; IntAct=EBI-1105310, EBI-722284;
CC Q9H1K0; Q9NRW7: VPS45; NbExp=4; IntAct=EBI-1105310, EBI-1782543;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side.
CC Early endosome membrane {ECO:0000269|PubMed:22308388}; Lipid-anchor.
CC Note=Enriched in endosomes that are in close proximity to clathrin-
CC enriched regions at the cell surface. {ECO:0000269|PubMed:22308388}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H1K0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H1K0-2; Sequence=VSP_056003, VSP_056004;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC03860.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAD92910.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY009133; AAG33246.1; -; mRNA.
DR EMBL; AK092312; BAC03860.1; ALT_INIT; mRNA.
DR EMBL; AK301735; BAG63200.1; -; mRNA.
DR EMBL; AC090954; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC106940; AAI06941.1; -; mRNA.
DR EMBL; AB209673; BAD92910.1; ALT_INIT; mRNA.
DR CCDS; CCDS2623.1; -. [Q9H1K0-1]
DR RefSeq; NP_001289307.1; NM_001302378.1. [Q9H1K0-1]
DR RefSeq; NP_071735.2; NM_022340.3. [Q9H1K0-1]
DR RefSeq; XP_005265441.1; XM_005265384.4. [Q9H1K0-1]
DR RefSeq; XP_005265442.1; XM_005265385.4. [Q9H1K0-1]
DR RefSeq; XP_016862512.1; XM_017007023.1. [Q9H1K0-1]
DR PDB; 1YZM; X-ray; 1.50 A; A=458-503.
DR PDB; 1Z0J; X-ray; 1.32 A; B=728-784.
DR PDB; 1Z0K; X-ray; 1.92 A; B/D=440-503.
DR PDBsum; 1YZM; -.
DR PDBsum; 1Z0J; -.
DR PDBsum; 1Z0K; -.
DR AlphaFoldDB; Q9H1K0; -.
DR SMR; Q9H1K0; -.
DR BioGRID; 122084; 48.
DR ELM; Q9H1K0; -.
DR IntAct; Q9H1K0; 25.
DR MINT; Q9H1K0; -.
DR STRING; 9606.ENSP00000253699; -.
DR GlyGen; Q9H1K0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H1K0; -.
DR PhosphoSitePlus; Q9H1K0; -.
DR BioMuta; RBSN; -.
DR DMDM; 108935884; -.
DR EPD; Q9H1K0; -.
DR jPOST; Q9H1K0; -.
DR MassIVE; Q9H1K0; -.
DR MaxQB; Q9H1K0; -.
DR PaxDb; Q9H1K0; -.
DR PeptideAtlas; Q9H1K0; -.
DR PRIDE; Q9H1K0; -.
DR ProteomicsDB; 5392; -.
DR ProteomicsDB; 80421; -. [Q9H1K0-1]
DR ABCD; Q9H1K0; 8 sequenced antibodies.
DR Antibodypedia; 26666; 205 antibodies from 33 providers.
DR DNASU; 64145; -.
DR Ensembl; ENST00000253699.7; ENSP00000253699.3; ENSG00000131381.12. [Q9H1K0-1]
DR Ensembl; ENST00000476527.6; ENSP00000422551.1; ENSG00000131381.12. [Q9H1K0-1]
DR GeneID; 64145; -.
DR KEGG; hsa:64145; -.
DR MANE-Select; ENST00000253699.7; ENSP00000253699.3; NM_022340.4; NP_071735.2.
DR UCSC; uc003bzm.1; human. [Q9H1K0-1]
DR CTD; 64145; -.
DR DisGeNET; 64145; -.
DR GeneCards; RBSN; -.
DR HGNC; HGNC:20759; RBSN.
DR HPA; ENSG00000131381; Low tissue specificity.
DR MalaCards; RBSN; -.
DR MIM; 609511; gene.
DR neXtProt; NX_Q9H1K0; -.
DR OpenTargets; ENSG00000131381; -.
DR Orphanet; 369852; Congenital neutropenia-myelofibrosis-nephromegaly syndrome.
DR PharmGKB; PA134959491; -.
DR VEuPathDB; HostDB:ENSG00000131381; -.
DR eggNOG; KOG1842; Eukaryota.
DR GeneTree; ENSGT00390000007159; -.
DR HOGENOM; CLU_020798_2_0_1; -.
DR InParanoid; Q9H1K0; -.
DR OMA; CNDCSKF; -.
DR PhylomeDB; Q9H1K0; -.
DR TreeFam; TF106125; -.
DR PathwayCommons; Q9H1K0; -.
DR Reactome; R-HSA-168138; Toll Like Receptor 9 (TLR9) Cascade.
DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; Q9H1K0; -.
DR SIGNOR; Q9H1K0; -.
DR BioGRID-ORCS; 64145; 184 hits in 1092 CRISPR screens.
DR ChiTaRS; RBSN; human.
DR EvolutionaryTrace; Q9H1K0; -.
DR GeneWiki; ZFYVE20; -.
DR GenomeRNAi; 64145; -.
DR Pharos; Q9H1K0; Tbio.
DR PRO; PR:Q9H1K0; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9H1K0; protein.
DR Bgee; ENSG00000131381; Expressed in endothelial cell and 189 other tissues.
DR ExpressionAtlas; Q9H1K0; baseline and differential.
DR Genevisible; Q9H1K0; HS.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; NAS:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR GO; GO:0034498; P:early endosome to Golgi transport; IMP:UniProtKB.
DR GO; GO:0016197; P:endosomal transport; NAS:UniProtKB.
DR GO; GO:0090160; P:Golgi to lysosome transport; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:1903358; P:regulation of Golgi organization; IMP:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR021565; Rbsn_Rab-bd.
DR InterPro; IPR036531; Rbsn_Rab-bd_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF11464; Rbsn; 2.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF140125; SSF140125; 2.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell membrane;
KW Coiled coil; Endosome; Lipoprotein; Membrane; Metal-binding;
KW Phosphoprotein; Protein transport; Reference proteome; Transport; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..784
FT /note="Rabenosyn-5"
FT /id="PRO_0000098711"
FT DOMAIN 496..515
FT /note="UIM"
FT /evidence="ECO:0000305"
FT ZN_FING 14..37
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 157..260
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 100..263
FT /note="Necessary for the correct targeting to endosomes"
FT REGION 207..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..784
FT /note="Necessary for interaction with EHD1"
FT /evidence="ECO:0000269|PubMed:15020713"
FT REGION 264..500
FT /note="Necessary for interaction with RAB4A"
FT REGION 390..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..784
FT /note="Necessary for interaction with RAB5A"
FT COILED 378..414
FT /evidence="ECO:0000255"
FT COILED 472..531
FT /evidence="ECO:0000255"
FT COMPBIAS 207..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..416
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 255
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80Y56"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 684
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 200..208
FT /note="NKLTSASKE -> KITTLHGES (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056003"
FT VAR_SEQ 209..784
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056004"
FT VARIANT 425
FT /note="G -> R (found in a patient with intractable
FT epileptic encephalopathy, developmental delay and
FT additional multi-organ symptoms; unknown pathological
FT significance; dbSNP:rs144008665)"
FT /evidence="ECO:0000269|PubMed:25233840"
FT /id="VAR_072416"
FT VARIANT 591
FT /note="L -> P (in dbSNP:rs9868848)"
FT /id="VAR_052982"
FT VARIANT 641
FT /note="T -> A (in dbSNP:rs9851219)"
FT /id="VAR_052983"
FT VARIANT 722
FT /note="M -> I (in dbSNP:rs9830744)"
FT /id="VAR_052984"
FT MUTAGEN 626..628
FT /note="NPF->APA: Reduces the interaction with EHD1.
FT Abolishes the interaction with EHD1; when associated with
FT 662-APA-664."
FT /evidence="ECO:0000269|PubMed:15020713"
FT MUTAGEN 662..664
FT /note="NPF->APA: Reduces the interaction with EHD1.
FT Abolishes the interaction with EHD1; when associated with
FT 626-APA-628."
FT /evidence="ECO:0000269|PubMed:15020713"
FT CONFLICT 106
FT /note="F -> L (in Ref. 1; AAG33246)"
FT /evidence="ECO:0000305"
FT CONFLICT 720
FT /note="F -> L (in Ref. 1; AAG33246)"
FT /evidence="ECO:0000305"
FT HELIX 458..475
FT /evidence="ECO:0007829|PDB:1YZM"
FT HELIX 479..500
FT /evidence="ECO:0007829|PDB:1YZM"
FT HELIX 736..755
FT /evidence="ECO:0007829|PDB:1Z0J"
FT HELIX 759..779
FT /evidence="ECO:0007829|PDB:1Z0J"
SQ SEQUENCE 784 AA; 88870 MW; D49E0E5A95B18616 CRC64;
MASLDDPGEV REGFLCPLCL KDLQSFYQLH SHYEEEHSGE DRDVKGQIKS LVQKAKKAKD
RLLKREGDDR AESGTQGYES FSYGGVDPYM WEPQELGAVR SHLSDFKKHR AARIDHYVVE
VNKLIIRLEK LTAFDRTNTE SAKIRAIEKS VVPWVNDQDV PFCPDCGNKF SIRNRRHHCR
LCGSIMCKKC MELISLPLAN KLTSASKESL STHTSPSQSP NSVHGSRRGS ISSMSSVSSV
LDEKDDDRIR CCTHCKDTLL KREQQIDEKE HTPDIVKLYE KLRLCMEKVD QKAPEYIRMA
ASLNAGETTY SLEHASDLRV EVQKVYELID ALSKKILTLG LNQDPPPHPS NLRLQRMIRY
SATLFVQEKL LGLMSLPTKE QFEELKKKRK EEMERKRAVE RQAALESQRR LEERQSGLAS
RAANGEVASL RRGPAPLRKA EGWLPLSGGQ GQSEDSDPLL QQIHNITSFI RQAKAAGRMD
EVRTLQENLR QLQDEYDQQQ TEKAIELSRR QAEEEDLQRE QLQMLREREL EREREQFRVA
SLHTRTRSLD FREIGPFQLE PSREPRTHLA YALDLGSSPV PSSTAPKTPS LSSTQPTRVW
SGPPAVGQER LPQSSMPQQH EGPSLNPFDE EDLSSPMEEA TTGPPAAGVS LDPSARILKE
YNPFEEEDEE EEAVAGNPFI QPDSPAPNPF SEEDEHPQQR LSSPLVPGNP FEEPTCINPF
EMDSDSGPEA EEPIEEELLL QQIDNIKAYI FDAKQCGRLD EVEVLTENLR ELKHTLAKQK
GGTD
