ID ANFY1_HUMAN Reviewed; 1169 AA. AC Q9P2R3; A8KA65; Q5RKV4; Q9ULG5; DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 04-AUG-2003, sequence version 2. DT 28-JAN-2026, entry version 194. DE RecName: Full=Ankyrin repeat and FYVE domain-containing protein 1 {ECO:0000312|HGNC:HGNC:20763}; DE AltName: Full=Ankyrin repeats hooked to a zinc finger motif; DE AltName: Full=Rab5-binding and ankyrin repeats-containing protein {ECO:0000303|PubMed:15328530}; DE Short=Rabankyrin-5 {ECO:0000303|PubMed:15328530}; DE Short=Rank-5 {ECO:0000303|PubMed:22284051}; GN Name=ANKFY1 {ECO:0000312|HGNC:HGNC:20763}; Synonyms=ANKHZN, KIAA1255; 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 {ECO:0000312|Proteomes:UP000005640}; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RC TISSUE=Fetal brain; RX PubMed=10940552; DOI=10.1016/s0378-1119(00)00247-x; RA Kuriyama H., Asakawa S., Minoshima S., Maruyama H., Ishii N., Ito K., RA Gejyo F., Arakawa M., Shimizu N., Kuwano R.; RT "Characterization and chromosomal mapping of a novel human gene, ANKHZN."; RL Gene 253:151-160(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND TISSUE SPECIFICITY. RC TISSUE=Brain; RX PubMed=10574462; DOI=10.1093/dnares/6.5.337; RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XV. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 6:337-345(1999). RN [3] RP SEQUENCE REVISION. RX PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Trachea; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-458 (ISOFORM 1). RC TISSUE=Mammary gland; 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 [8] RP PROTEIN SEQUENCE OF 2-11; 145-151 AND 924-931, CLEAVAGE OF INITIATOR RP METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lung carcinoma; RA Bienvenut W.V., Vousden K.H., Lukashchuk N.; RL Submitted (MAR-2008) to UniProtKB. RN [9] RP FUNCTION, INTERACTION WITH RAB5A, AND SUBCELLULAR LOCATION. RX PubMed=15328530; DOI=10.1371/journal.pbio.0020261; RA Schnatwinkel C., Christoforidis S., Lindsay M.R., Uttenweiler-Joseph S., RA Wilm M., Parton R.G., Zerial M.; RT "The Rab5 effector Rabankyrin-5 regulates and coordinates different RT endocytic mechanisms."; RL PLoS Biol. 2:E261-E261(2004). RN [10] 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 [11] RP FUNCTION, INTERACTION WITH EHD1 AND VPS26A, SUBCELLULAR LOCATION, AND RP MUTAGENESIS OF 421-ASN--PHE-423 AND 424-GLU-ASP-425. RX PubMed=22284051; DOI=10.1111/j.1600-0854.2012.01334.x; RA Zhang J., Reiling C., Reinecke J.B., Prislan I., Marky L.A., Sorgen P.L., RA Naslavsky N., Caplan S.; RT "Rabankyrin-5 interacts with EHD1 and Vps26 to regulate endocytic RT trafficking and retromer function."; RL Traffic 13:745-757(2012). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; 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 FUNCTION IN ENDOSOMAL TRAFFICKING AND RECEPTOR INTERNALIZATION, AND RP INTERACTION WITH RHOD. RX PubMed=24102721; DOI=10.1111/tra.12121; RA Nehru V., Voytyuk O., Lennartsson J., Aspenstroem P.; RT "RhoD binds the Rab5 effector Rabankyrin-5 and has a role in trafficking of RT the platelet-derived growth factor receptor."; RL Traffic 14:1242-1254(2013). RN [14] RP IDENTIFICATION BY 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 [15] RP FUNCTION, INTERACTION WITH RAB5A AND GAPVD1, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, DOMAIN FYVE, AND VARIANT LEU-53. RX PubMed=29959197; DOI=10.1681/asn.2017121312; RA Hermle T., Schneider R., Schapiro D., Braun D.A., van der Ven A.T., RA Warejko J.K., Daga A., Widmeier E., Nakayama M., Jobst-Schwan T., RA Majmundar A.J., Ashraf S., Rao J., Finn L.S., Tasic V., Hernandez J.D., RA Bagga A., Jalalah S.M., El Desoky S., Kari J.A., Laricchia K.M., Lek M., RA Rehm H.L., MacArthur D.G., Mane S., Lifton R.P., Shril S., Hildebrandt F.; RT "GAPVD1 and ANKFY1 Mutations Implicate RAB5 Regulation in Nephrotic RT Syndrome."; RL J. Am. Soc. Nephrol. 29:2123-2138(2018). CC -!- FUNCTION: Proposed effector of Rab5 (PubMed:15328530). Binds to CC phosphatidylinositol 3-phosphate (PI[3]P) (PubMed:15328530). Involved CC in homotypic early endosome fusion and to a lesser extent in CC heterotypic fusion of clathrin-coated vesicles with early endosomes CC (PubMed:15328530). Involved in macropinocytosis; the function is CC dependent on Rab5-GTP (PubMed:15328530). Required for correct endosomal CC localization (PubMed:15328530). Involved in the internalization and CC trafficking of activated tyrosine kinase receptors such as PDGFRB CC (PubMed:24102721). Regulates the subcellular localization of the CC retromer complex in a EHD1-dependent manner (PubMed:22284051). Involved CC in endosome-to-Golgi transport and biosynthetic transport to late CC endosomes and lysosomes indicative for a regulation of retromer CC complex-mediated retrograde transport (PubMed:22284051). Required for CC podocyte migration (PubMed:29959197). {ECO:0000269|PubMed:15328530, CC ECO:0000269|PubMed:22284051, ECO:0000269|PubMed:24102721, CC ECO:0000269|PubMed:29959197}. CC -!- SUBUNIT: Interacts with RAB5A (in GTP-bound form) (PubMed:15328530, CC PubMed:29959197). Interacts with RHOD (independent of GTP-loaded CC status) (PubMed:24102721). Interacts (via NPF motif) with EHD1 (via EH CC domain) (PubMed:22284051). Interacts with VPS26A and VPS35; the CC interaction is independent of EHD1 and is indicative for an association CC with the cargo recognition subcomplex of the retromer complex CC (PubMed:22284051). Interacts with GAPVD1 (PubMed:29959197). CC {ECO:0000269|PubMed:15328530, ECO:0000269|PubMed:22284051, CC ECO:0000269|PubMed:24102721, ECO:0000269|PubMed:29959197}. CC -!- INTERACTION: CC Q9P2R3; Q9H4M9: EHD1; NbExp=8; IntAct=EBI-2513908, EBI-490691; CC Q9P2R3; Q9NZN3: EHD3; NbExp=3; IntAct=EBI-2513908, EBI-2870749; CC Q9P2R3; P60520: GABARAPL2; NbExp=2; IntAct=EBI-2513908, EBI-720116; CC Q9P2R3; P20339: RAB5A; NbExp=2; IntAct=EBI-2513908, EBI-399437; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10940552}. Endosome CC membrane {ECO:0000269|PubMed:10940552}; Peripheral membrane protein CC {ECO:0000269|PubMed:10940552}. Early endosome CC {ECO:0000269|PubMed:15328530, ECO:0000269|PubMed:22284051, CC ECO:0000269|PubMed:29959197}. Note=Also associated with endosomal CC membranes. Localizes to macropinosomes (PubMed:15328530). On endosomes, CC partially colocalizes with components of the retromer CC (PubMed:22284051). {ECO:0000269|PubMed:15328530, CC ECO:0000269|PubMed:22284051}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9P2R3-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9P2R3-2; Sequence=VSP_035607; CC Name=4; CC IsoId=Q9P2R3-4; Sequence=VSP_041447; CC -!- TISSUE SPECIFICITY: High expression in whole adult brain and CC intermediate expression in all other tissues and specific brain regions CC examined, including fetal brain (PubMed:10574462, PubMed:10940552). CC Expressed in podocytes (at protein level) (PubMed:29959197). CC {ECO:0000269|PubMed:10574462, ECO:0000269|PubMed:10940552, CC ECO:0000269|PubMed:29959197}. CC -!- DOMAIN: The FYVE-type zinc finger domain is required for endosomal CC localization. {ECO:0000269|PubMed:29959197}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH52308.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305}; CC Sequence=BAA86569.2; Type=Erroneous initiation; Note=Extended N-terminus.; 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; AB037360; BAA90300.1; -; mRNA. DR EMBL; AB033081; BAA86569.2; ALT_INIT; mRNA. DR EMBL; AK292930; BAF85619.1; -; mRNA. DR EMBL; AC087292; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC087742; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471108; EAW90448.1; -; Genomic_DNA. DR EMBL; BC052308; AAH52308.1; ALT_SEQ; mRNA. DR CCDS; CCDS42236.1; -. [Q9P2R3-2] DR CCDS; CCDS58502.1; -. [Q9P2R3-4] DR CCDS; CCDS82038.1; -. [Q9P2R3-1] DR RefSeq; NP_001244928.1; NM_001257999.3. [Q9P2R3-4] DR RefSeq; NP_001316992.1; NM_001330063.2. [Q9P2R3-1] DR RefSeq; NP_057460.3; NM_016376.4. [Q9P2R3-2] DR AlphaFoldDB; Q9P2R3; -. DR SMR; Q9P2R3; -. DR BioGRID; 119564; 265. DR DIP; DIP-46068N; -. DR FunCoup; Q9P2R3; 3866. DR IntAct; Q9P2R3; 49. DR MINT; Q9P2R3; -. DR STRING; 9606.ENSP00000459943; -. DR GlyGen; Q9P2R3; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site). DR iPTMnet; Q9P2R3; -. DR MetOSite; Q9P2R3; -. DR PhosphoSitePlus; Q9P2R3; -. DR SwissPalm; Q9P2R3; -. DR BioMuta; ANKFY1; -. DR DMDM; 33514905; -. DR jPOST; Q9P2R3; -. DR MassIVE; Q9P2R3; -. DR PaxDb; 9606-ENSP00000459943; -. DR PeptideAtlas; Q9P2R3; -. DR ProteomicsDB; 83880; -. [Q9P2R3-1] DR ProteomicsDB; 83881; -. [Q9P2R3-2] DR ProteomicsDB; 83882; -. [Q9P2R3-4] DR Pumba; Q9P2R3; -. DR Antibodypedia; 5541; 92 antibodies from 19 providers. DR DNASU; 51479; -. DR Ensembl; ENST00000341657.9; ENSP00000343362.4; ENSG00000185722.19. [Q9P2R3-1] DR Ensembl; ENST00000570535.5; ENSP00000459943.1; ENSG00000185722.19. [Q9P2R3-4] DR Ensembl; ENST00000574367.5; ENSP00000459775.1; ENSG00000185722.19. [Q9P2R3-2] DR Ensembl; ENST00000648043.1; ENSP00000497187.1; ENSG00000185722.19. [Q9P2R3-1] DR GeneID; 51479; -. DR KEGG; hsa:51479; -. DR MANE-Select; ENST00000341657.9; ENSP00000343362.4; NM_001330063.2; NP_001316992.1. DR UCSC; uc002fxn.4; human. [Q9P2R3-1] DR AGR; HGNC:20763; -. DR ClinPGx; PA134984226; -. DR CTD; 51479; -. DR DisGeNET; 51479; -. DR GeneCards; ANKFY1; -. DR HGNC; HGNC:20763; ANKFY1. DR HPA; ENSG00000185722; Low tissue specificity. DR MalaCards; ANKFY1; -. DR MIM; 607927; gene. DR OpenTargets; ENSG00000185722; -. DR Orphanet; 656; Hereditary steroid-resistant nephrotic syndrome. DR VEuPathDB; HostDB:ENSG00000185722; -. DR eggNOG; KOG0504; Eukaryota. DR eggNOG; KOG4591; Eukaryota. DR GeneTree; ENSGT00940000156179; -. DR HOGENOM; CLU_010618_0_0_1; -. DR InParanoid; Q9P2R3; -. DR OMA; WGLEQVV; -. DR OrthoDB; 2306477at2759; -. DR PAN-GO; Q9P2R3; 4 GO annotations based on evolutionary models. DR PhylomeDB; Q9P2R3; -. DR PathwayCommons; Q9P2R3; -. DR Reactome; R-HSA-9013405; RHOD GTPase cycle. DR SignaLink; Q9P2R3; -. DR SIGNOR; Q9P2R3; -. DR Agora; ENSG00000185722; -. DR BioGRID-ORCS; 51479; 21 hits in 1198 CRISPR screens. DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities. DR ChiTaRS; ANKFY1; human. DR GeneWiki; ANKFY1; -. DR GenomeRNAi; 51479; -. DR Pharos; Q9P2R3; Tbio. DR PRO; PR:Q9P2R3; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q9P2R3; protein. DR Bgee; ENSG00000185722; Expressed in skin of hip and 183 other cell types or tissues. DR ExpressionAtlas; Q9P2R3; baseline and differential. DR GO; GO:0005829; C:cytosol; IEA:GOC. DR GO; GO:0005769; C:early endosome; IDA:UniProtKB. DR GO; GO:0005768; C:endosome; IDA:HPA. DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB. DR GO; GO:0044354; C:macropinosome; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; IDA:UniProtKB. DR GO; GO:0031267; F:small GTPase binding; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW. DR GO; GO:0016197; P:endosomal transport; IMP:UniProtKB. DR GO; GO:0034058; P:endosomal vesicle fusion; IDA:UniProtKB. DR GO; GO:0090160; P:Golgi to lysosome transport; IMP:UniProtKB. DR GO; GO:0048549; P:positive regulation of pinocytosis; IDA:UniProtKB. DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:UniProtKB. DR CDD; cd18501; BACK_ANKFY1_Rank5; 1. DR CDD; cd18303; BTB_POZ_Rank-5; 1. DR CDD; cd15728; FYVE_ANFY1; 1. DR FunFam; 1.25.40.20:FF:000116; Ankyrin repeat and FYVE domain containing 1; 1. DR FunFam; 1.25.40.20:FF:000142; Ankyrin repeat and FYVE domain containing 1; 1. DR FunFam; 1.25.40.20:FF:000184; Ankyrin repeat and FYVE domain containing 1; 1. DR FunFam; 1.25.40.20:FF:000210; Ankyrin repeat and FYVE domain containing 1; 1. DR FunFam; 3.30.40.10:FF:000104; Ankyrin repeat and FYVE domain-containing 1; 1. DR FunFam; 3.30.710.10:FF:000086; Ankyrin repeat and FYVE domain-containing 1; 1. DR FunFam; 1.25.40.20:FF:000166; rabankyrin-5 isoform X1; 1. DR FunFam; 1.25.40.20:FF:000469; rabankyrin-5 isoform X1; 1. DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 6. DR Gene3D; 3.30.710.10; Potassium Channel Kv1.1, Chain A; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR049765; ANFY1_BTB_POZ. DR InterPro; IPR049764; ANFY1_FYVE. DR InterPro; IPR049763; ANKFY1_BACK. DR InterPro; IPR002110; Ankyrin_rpt. DR InterPro; IPR036770; Ankyrin_rpt-contain_sf. DR InterPro; IPR000210; BTB/POZ_dom. DR InterPro; IPR051165; Multifunctional_ANK_Repeat. DR InterPro; IPR011333; SKP1/BTB/POZ_sf. 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; PTHR24123:SF130; ANKYRIN REPEAT AND FYVE DOMAIN CONTAINING 1; 1. DR PANTHER; PTHR24123; ANKYRIN REPEAT-CONTAINING; 1. DR Pfam; PF00023; Ank; 1. DR Pfam; PF12796; Ank_2; 5. DR Pfam; PF13637; Ank_4; 1. DR Pfam; PF00651; BTB; 1. DR Pfam; PF01363; FYVE; 1. DR PRINTS; PR01415; ANKYRIN. DR SMART; SM00248; ANK; 21. DR SMART; SM00225; BTB; 1. DR SMART; SM00064; FYVE; 1. DR SUPFAM; SSF48403; Ankyrin repeat; 3. DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1. DR SUPFAM; SSF54695; POZ domain; 1. DR PROSITE; PS50297; ANK_REP_REGION; 8. DR PROSITE; PS50088; ANK_REPEAT; 13. DR PROSITE; PS50097; BTB; 1. DR PROSITE; PS50178; ZF_FYVE; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; ANK repeat; Coiled coil; Cytoplasm; KW Direct protein sequencing; Disease variant; Endocytosis; Endosome; KW Membrane; Metal-binding; Phosphoprotein; Proteomics identification; KW Reference proteome; Repeat; Zinc; Zinc-finger. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.8" FT CHAIN 2..1169 FT /note="Ankyrin repeat and FYVE domain-containing protein 1" FT /id="PRO_0000066890" FT DOMAIN 68..130 FT /note="BTB" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037" FT REPEAT 217..247 FT /note="ANK 1" FT /evidence="ECO:0000255" FT REPEAT 255..284 FT /note="ANK 2" FT /evidence="ECO:0000255" FT REPEAT 288..317 FT /note="ANK 3" FT /evidence="ECO:0000255" FT REPEAT 322..362 FT /note="ANK 4" FT /evidence="ECO:0000255" FT REPEAT 366..396 FT /note="ANK 5" FT /evidence="ECO:0000255" FT REPEAT 490..519 FT /note="ANK 6" FT /evidence="ECO:0000255" FT REPEAT 542..572 FT /note="ANK 7" FT /evidence="ECO:0000255" FT REPEAT 588..617 FT /note="ANK 8" FT /evidence="ECO:0000255" FT REPEAT 621..650 FT /note="ANK 9" FT /evidence="ECO:0000255" FT REPEAT 654..683 FT /note="ANK 10" FT /evidence="ECO:0000255" FT REPEAT 687..716 FT /note="ANK 11" FT /evidence="ECO:0000255" FT REPEAT 724..753 FT /note="ANK 12" FT /evidence="ECO:0000255" FT REPEAT 769..798 FT /note="ANK 13" FT /evidence="ECO:0000255" FT REPEAT 802..832 FT /note="ANK 14" FT /evidence="ECO:0000255" FT REPEAT 836..865 FT /note="ANK 15" FT /evidence="ECO:0000255" FT REPEAT 870..899 FT /note="ANK 16" FT /evidence="ECO:0000255" FT REPEAT 905..934 FT /note="ANK 17" FT /evidence="ECO:0000255" FT REPEAT 938..967 FT /note="ANK 18" FT /evidence="ECO:0000255" FT REPEAT 971..1001 FT /note="ANK 19" FT /evidence="ECO:0000255" FT REPEAT 1005..1037 FT /note="ANK 20" FT /evidence="ECO:0000255" FT REPEAT 1043..1072 FT /note="ANK 21" FT /evidence="ECO:0000255" FT ZN_FING 1104..1164 FT /note="FYVE-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT REGION 650..759 FT /note="Interaction with RHOD and RAB5A" FT /evidence="ECO:0000269|PubMed:24102721" FT COILED 6..40 FT /evidence="ECO:0000255" FT MOTIF 421..423 FT /note="NPF" FT BINDING 1110 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 1113 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 1126 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 1129 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 1134 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 1137 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 1156 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 1159 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:0000269|Ref.8" FT MOD_RES 270 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..4 FT /note="MAEE -> MPTPRDCGRLRSRAGRSRAGAACSRGAPRAAREALDCRRCRDAG FT GK (in isoform 4)" FT /evidence="ECO:0000303|PubMed:10574462" FT /id="VSP_041447" FT VAR_SEQ 650 FT /note="V -> VS (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_035607" FT VARIANT 53 FT /note="R -> L (found in 2 patients with a form of FT steroid-resistant nephrotic syndrome; reduces binding FT affinity for GTP-bound RAB5A; may alter the endocytic FT trafficking of NPHS1/Nephrin; no adverse effect on FT endosomal localization; fails to rescue podocyte migration FT phenotype in shRNA-mediated knockdown cells)" FT /evidence="ECO:0000269|PubMed:29959197" FT /id="VAR_090508" FT MUTAGEN 421..423 FT /note="NPF->APA: Disrupts interaction with EHD1." FT /evidence="ECO:0000269|PubMed:22284051" FT MUTAGEN 424..425 FT /note="ED->AA: Decreases interaction with EHD1." FT /evidence="ECO:0000269|PubMed:22284051" FT CONFLICT 48 FT /note="E -> K (in Ref. 1; BAA90300)" FT /evidence="ECO:0000305" FT CONFLICT 115 FT /note="M -> V (in Ref. 1; BAA90300)" FT /evidence="ECO:0000305" FT CONFLICT 207 FT /note="A -> P (in Ref. 1; BAA90300)" FT /evidence="ECO:0000305" FT CONFLICT 235 FT /note="F -> S (in Ref. 1; BAA90300)" FT /evidence="ECO:0000305" FT CONFLICT 270 FT /note="S -> N (in Ref. 1; BAA90300)" FT /evidence="ECO:0000305" FT CONFLICT 283..291 FT /note="DMVDKSGWS -> AWWPRVLE (in Ref. 1; BAA90300)" FT /evidence="ECO:0000305" FT CONFLICT 299..300 FT /note="RG -> E (in Ref. 1; BAA90300)" FT /evidence="ECO:0000305" FT CONFLICT 322 FT /note="A -> C (in Ref. 1; BAA90300)" FT /evidence="ECO:0000305" FT CONFLICT 336..337 FT /note="KK -> RN (in Ref. 1; BAA90300)" FT /evidence="ECO:0000305" FT CONFLICT 379 FT /note="N -> D (in Ref. 1; BAA90300)" FT /evidence="ECO:0000305" FT CONFLICT 385 FT /note="Q -> H (in Ref. 1; BAA90300)" FT /evidence="ECO:0000305" FT CONFLICT 645 FT /note="Q -> R (in Ref. 1; BAA90300)" FT /evidence="ECO:0000305" FT CONFLICT 652..654 FT /note="TQD -> PQA (in Ref. 1; BAA90300)" FT /evidence="ECO:0000305" FT CONFLICT 687 FT /note="K -> E (in Ref. 1; BAA90300)" FT /evidence="ECO:0000305" FT CONFLICT 713 FT /note="D -> G (in Ref. 1; BAA90300)" FT /evidence="ECO:0000305" FT CONFLICT 784 FT /note="Missing (in Ref. 1; BAA90300)" FT /evidence="ECO:0000305" FT CONFLICT 795 FT /note="N -> D (in Ref. 1; BAA90300)" FT /evidence="ECO:0000305" FT CONFLICT 798 FT /note="A -> P (in Ref. 1; BAA90300)" FT /evidence="ECO:0000305" FT CONFLICT 807 FT /note="I -> C (in Ref. 1; BAA90300)" FT /evidence="ECO:0000305" FT CONFLICT 827..829 FT /note="DIH -> ISS (in Ref. 1; BAA90300)" FT /evidence="ECO:0000305" FT CONFLICT 835 FT /note="R -> K (in Ref. 1; BAA90300)" FT /evidence="ECO:0000305" FT CONFLICT 849 FT /note="N -> D (in Ref. 1; BAA90300)" FT /evidence="ECO:0000305" FT CONFLICT 860 FT /note="E -> G (in Ref. 1; BAA90300)" FT /evidence="ECO:0000305" FT CONFLICT 874 FT /note="F -> S (in Ref. 1; BAA90300)" FT /evidence="ECO:0000305" FT CONFLICT 889 FT /note="F -> S (in Ref. 1; BAA90300)" FT /evidence="ECO:0000305" FT CONFLICT 901 FT /note="V -> A (in Ref. 1; BAA90300)" FT /evidence="ECO:0000305" FT CONFLICT 905 FT /note="S -> P (in Ref. 1; BAA90300)" FT /evidence="ECO:0000305" FT CONFLICT 913 FT /note="A -> V (in Ref. 1; BAA90300)" FT /evidence="ECO:0000305" FT CONFLICT 916 FT /note="A -> E (in Ref. 1; BAA90300)" FT /evidence="ECO:0000305" FT CONFLICT 933 FT /note="N -> T (in Ref. 1; BAA90300)" FT /evidence="ECO:0000305" FT CONFLICT 940 FT /note="Q -> K (in Ref. 1; BAA90300)" FT /evidence="ECO:0000305" FT CONFLICT 949 FT /note="Q -> E (in Ref. 1; BAA90300)" FT /evidence="ECO:0000305" FT CONFLICT 962 FT /note="G -> A (in Ref. 1; BAA90300)" FT /evidence="ECO:0000305" FT CONFLICT 1120 FT /note="T -> A (in Ref. 1; BAA90300)" FT /evidence="ECO:0000305" FT CONFLICT 1157 FT /note="N -> T (in Ref. 1; BAA90300)" FT /evidence="ECO:0000305" SQ SEQUENCE 1169 AA; 128399 MW; 589297CA4ACDDB56 CRC64; MAEEEVAKLE KHLMLLRQEY VKLQKKLAET EKRCALLAAQ ANKESSSESF ISRLLAIVAD LYEQEQYSDL KIKVGDRHIS AHKFVLAARS DSWSLANLSS TKELDLSDAN PEVTMTMLRW IYTDELEFRE DDVFLTELMK LANRFQLQLL RERCEKGVMS LVNVRNCIRF YQTAEELNAS TLMNYCAEII ASHWDDLRKE DFSSMSAQLL YKMIKSKTEY PLHKAIKVER EDVVFLYLIE MDSQLPGKLN EADHNGDLAL DLALSRRLES IATTLVSHKA DVDMVDKSGW SLLHKGIQRG DLFAATFLIK NGAFVNAATL GAQETPLHLV ALYSSKKHSA DVMSEMAQIA EALLQAGANP NMQDSKGRTP LHVSIMAGNE YVFSQLLQCK QLDLELKDHE GSTALWLAVQ HITVSSDQSV NPFEDVPVVN GTSFDENSFA ARLIQRGSHT DAPDTATGNC LLQRAAGAGN EAAALFLATN GAHVNHRNKW GETPLHTACR HGLANLTAEL LQQGANPNLQ TEEALPLPKE AASLTSLADS VHLQTPLHMA IAYNHPDVVS VILEQKANAL HATNNLQIIP DFSLKDSRDQ TVLGLALWTG MHTIAAQLLG SGAAINDTMS DGQTLLHMAI QRQDSKSALF LLEHQADINV RTQDGETALQ LAIRNQLPLV VDAICTRGAD MSVPDEKGNP PLWLALANNL EDIASTLVRH GCDATCWGPG PGGCLQTLLH RAIDENNEPT ACFLIRSGCD VNSPRQPGAN GEGEEEARDG QTPLHLAASW GLEETVQCLL EFGANVNAQD AEGRTPIHVA ISSQHGVIIQ LLVSHPDIHL NVRDRQGLTP FACAMTFKNN KSAEAILKRE SGAAEQVDNK GRNFLHVAVQ NSDIESVLFL ISVHANVNSR VQDASKLTPL HLAVQAGSEI IVRNLLLAGA KVNELTKHRQ TALHLAAQQD LPTICSVLLE NGVDFAAVDE NGNNALHLAV MHGRLNNIRV LLTECTVDAE AFNLRGQSPL HILGQYGKEN AAAIFDLFLE CMPGYPLDKP DADGSTVLLL AYMKGNANLC RAIVRSGARL GVNNNQGVNI FNYQVATKQL LFRLLDMLSK EPPWCDGSYC YECTARFGVT TRKHHCRHCG RLLCHKCSTK EIPIIKFDLN KPVRVCNICF DVLTLGGVS //