ANFY1_HUMAN
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 03-AUG-2022, entry version 177.
DE RecName: Full=Rabankyrin-5 {ECO:0000303|PubMed:15328530};
DE Short=Rank-5 {ECO:0000303|PubMed:22284051};
DE AltName: Full=Ankyrin repeat and FYVE domain-containing protein 1;
DE AltName: Full=Ankyrin repeats hooked to a zinc finger motif;
GN Name=ANKFY1; 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;
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, AND MUTAGENESIS OF
RP 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).
CC -!- FUNCTION: Proposed effector of Rab5. Binds to phosphatidylinositol 3-
CC phosphate (PI(3)P). Involved in homotypic early endosome fusion and to
CC a lesser extent in heterotypic fusion of chlathrin-coated vesicles with
CC early endosomes. Involved in macropinocytosis; the function is
CC dependent on Rab5-GTP. Required for correct endosomal localization.
CC Involved in the internalization and trafficking of activated tyrosine
CC kinase receptors such as PDGFRB. Regulates the subcellular localization
CC of the retromer complex in a EHD1-dependent manner. Involved in
CC endosome-to-Golgi transport and biosynthetic transport to late
CC endosomes and lysosomes indicative for a regulation of retromer
CC complex-mediated retrograde transport. {ECO:0000269|PubMed:15328530,
CC ECO:0000269|PubMed:22284051, ECO:0000269|PubMed:24102721}.
CC -!- SUBUNIT: Interacts with RAB5A (in GTP-bound form). Interacts with RHOD
CC (independent of GTP-loaded status). Interacts with EHD1. Interacts with
CC VPS26A; the interaction is independent of EHD1 and is indicative for an
CC association with the cargo recognition subcomplex of the retromer
CC complex. {ECO:0000269|PubMed:15328530, ECO:0000269|PubMed:22284051,
CC ECO:0000269|PubMed:24102721}.
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}. Note=Also associated with endosomal
CC membranes. Localizes to macropinosomes. {ECO:0000269|PubMed:15328530}.
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. {ECO:0000269|PubMed:10574462,
CC ECO:0000269|PubMed:10940552}.
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};
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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_001257999.2. [Q9P2R3-4]
DR RefSeq; NP_001316992.1; NM_001330063.1. [Q9P2R3-1]
DR RefSeq; NP_057460.3; NM_016376.4. [Q9P2R3-2]
DR AlphaFoldDB; Q9P2R3; -.
DR SMR; Q9P2R3; -.
DR BioGRID; 119564; 219.
DR DIP; DIP-46068N; -.
DR IntAct; Q9P2R3; 32.
DR MINT; Q9P2R3; -.
DR STRING; 9606.ENSP00000459943; -.
DR iPTMnet; Q9P2R3; -.
DR MetOSite; Q9P2R3; -.
DR PhosphoSitePlus; Q9P2R3; -.
DR BioMuta; ANKFY1; -.
DR DMDM; 33514905; -.
DR EPD; Q9P2R3; -.
DR jPOST; Q9P2R3; -.
DR MassIVE; Q9P2R3; -.
DR MaxQB; Q9P2R3; -.
DR PaxDb; Q9P2R3; -.
DR PeptideAtlas; Q9P2R3; -.
DR PRIDE; Q9P2R3; -.
DR ProteomicsDB; 83880; -. [Q9P2R3-1]
DR ProteomicsDB; 83881; -. [Q9P2R3-2]
DR ProteomicsDB; 83882; -. [Q9P2R3-4]
DR Antibodypedia; 5541; 92 antibodies from 20 providers.
DR DNASU; 51479; -.
DR Ensembl; ENST00000341657.9; ENSP00000343362.4; ENSG00000185722.18. [Q9P2R3-1]
DR Ensembl; ENST00000570535.5; ENSP00000459943.1; ENSG00000185722.18. [Q9P2R3-4]
DR Ensembl; ENST00000574367.5; ENSP00000459775.1; ENSG00000185722.18. [Q9P2R3-2]
DR Ensembl; ENST00000648043.1; ENSP00000497187.1; ENSG00000185722.18. [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 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 neXtProt; NX_Q9P2R3; -.
DR OpenTargets; ENSG00000185722; -.
DR Orphanet; 656; Genetic steroid-resistant nephrotic syndrome.
DR PharmGKB; PA134984226; -.
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; GPEGCQQ; -.
DR OrthoDB; 1115202at2759; -.
DR PhylomeDB; Q9P2R3; -.
DR TreeFam; TF351263; -.
DR PathwayCommons; Q9P2R3; -.
DR Reactome; R-HSA-9013405; RHOD GTPase cycle.
DR SignaLink; Q9P2R3; -.
DR BioGRID-ORCS; 51479; 18 hits in 1120 CRISPR screens.
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 181 other tissues.
DR ExpressionAtlas; Q9P2R3; baseline and differential.
DR Genevisible; Q9P2R3; HS.
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:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IDA:UniProtKB.
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 Gene3D; 1.25.40.20; -; 6.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR000210; BTB/POZ_dom.
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 Pfam; PF00023; Ank; 2.
DR Pfam; PF12796; Ank_2; 3.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF13857; Ank_5; 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; SSF48403; 3.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 12.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ANK repeat; Cytoplasm;
KW Direct protein sequencing; Endocytosis; Endosome; Membrane; Metal-binding;
KW Phosphoprotein; 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="Rabankyrin-5"
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 REPEAT 255..284
FT /note="ANK 2"
FT REPEAT 288..317
FT /note="ANK 3"
FT REPEAT 322..362
FT /note="ANK 4"
FT REPEAT 366..396
FT /note="ANK 5"
FT REPEAT 490..519
FT /note="ANK 6"
FT REPEAT 542..572
FT /note="ANK 7"
FT REPEAT 588..617
FT /note="ANK 8"
FT REPEAT 621..650
FT /note="ANK 9"
FT REPEAT 654..683
FT /note="ANK 10"
FT REPEAT 687..716
FT /note="ANK 11"
FT REPEAT 724..753
FT /note="ANK 12"
FT REPEAT 769..798
FT /note="ANK 13"
FT REPEAT 802..832
FT /note="ANK 14"
FT REPEAT 836..865
FT /note="ANK 15"
FT REPEAT 870..899
FT /note="ANK 16"
FT REPEAT 905..934
FT /note="ANK 17"
FT REPEAT 938..967
FT /note="ANK 18"
FT REPEAT 971..1001
FT /note="ANK 19"
FT REPEAT 1005..1037
FT /note="ANK 20"
FT REPEAT 1043..1072
FT /note="ANK 21"
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 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 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
