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 27-MAR-2024, entry version 188. 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}; 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; 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; 62. DR ELM; Q9H1K0; -. DR IntAct; Q9H1K0; 30. DR MINT; Q9H1K0; -. DR STRING; 9606.ENSP00000253699; -. DR GlyCosmos; Q9H1K0; 1 site, 1 glycan. DR GlyGen; Q9H1K0; 2 sites, 1 O-linked glycan (2 sites). 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; 9606-ENSP00000253699; -. DR PeptideAtlas; Q9H1K0; -. DR ProteomicsDB; 5392; -. DR ProteomicsDB; 80421; -. [Q9H1K0-1] DR Pumba; Q9H1K0; -. DR ABCD; Q9H1K0; 4 sequenced antibodies. DR Antibodypedia; 26666; 230 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 AGR; HGNC:20759; -. 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; CEHCLWL; -. DR OrthoDB; 1441111at2759; -. 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; 192 hits in 1169 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 191 other cell types or tissues. DR ExpressionAtlas; Q9H1K0; baseline and differential. 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 CDD; cd15716; FYVE_RBNS5; 1. DR Gene3D; 4.10.860.20; Rabenosyn, Rab binding domain; 2. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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 PANTHER; PTHR13510; FYVE-FINGER-CONTAINING RAB5 EFFECTOR PROTEIN RABENOSYN-5-RELATED; 1. DR PANTHER; PTHR13510:SF44; RABENOSYN-5; 1. DR Pfam; PF01363; FYVE; 1. DR Pfam; PF16601; NPF; 1. DR Pfam; PF11464; Rbsn; 2. DR SMART; SM00064; FYVE; 1. DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1. DR SUPFAM; SSF140125; Rabenosyn-5 Rab-binding domain-like; 2. DR PROSITE; PS50178; ZF_FYVE; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1. DR Genevisible; Q9H1K0; HS. 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; uncertain significance; FT 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 //