ANFY1_MOUSE
ID ANFY1_MOUSE Reviewed; 1169 AA.
AC Q810B6; B1ATS3; O54807; Q80TG6; Q80UH8;
DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Rabankyrin-5 {ECO:0000303|PubMed:15328530};
DE Short=Rank-5;
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND SUBCELLULAR LOCATION.
RX PubMed=10092534; DOI=10.1006/bbrc.1999.0430;
RA Ito K., Ishii N., Miyashita A., Tominaga K., Kuriyama H., Maruyama H.,
RA Shirai M., Naito M., Arakawa M., Kuwano R.;
RT "Molecular cloning of a novel 130-kDa cytoplasmic protein, Ankhzn,
RT containing ankyrin repeats hooked to a zinc finger motif.";
RL Biochem. Biophys. Res. Commun. 257:206-213(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), AND SEQUENCE
RP REVISION.
RA Maruyama H., Kuriyama H., Ishii N., Ito K., Odani S., Kuwano R.;
RT "Genomic organization, alternative splicing, and promoter assay of the
RT mouse Ankhzn gene.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
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 994-1169 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [6]
RP FUNCTION, 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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. Required for correct endosomal localization. Involved
CC in the internalization and trafficking of activated tyrosine kinase
CC receptors such as PDGFRB. Regulates the subcellular localization of the
CC retromer complex in a EHD1-dependent manner. Involved in endosome-to-
CC Golgi transport and biosynthetic transport to late endosomes and
CC lysosomes indicative for a regulation of retromer complex-mediated
CC retrograde transport (By similarity). Involved in macropinocytosis; the
CC function is dependent on Rab5-GTP. {ECO:0000250|UniProtKB:Q9P2R3,
CC ECO:0000269|PubMed:15328530}.
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:0000250|UniProtKB:Q9P2R3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10092534}. Endosome
CC membrane {ECO:0000269|PubMed:10092534}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10092534}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:15328530}. Note=Also associated with endosomal
CC membranes. Localizes to macropinosomes. In kidney proximal tubule cells
CC localizes to vesicle-like structures underneath the apical brush
CC border. {ECO:0000269|PubMed:15328530}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q810B6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q810B6-2; Sequence=VSP_007917, VSP_007918;
CC -!- TISSUE SPECIFICITY: Expressed in kidney proximal tubule epithelial
CC cells; at protein level. {ECO:0000269|PubMed:15328530}.
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DR EMBL; AB011370; BAA24980.2; -; mRNA.
DR EMBL; AB098329; BAC67211.1; -; mRNA.
DR EMBL; AB098157; BAC67389.1; -; Genomic_DNA.
DR EMBL; AB098157; BAC67388.1; -; Genomic_DNA.
DR EMBL; AL663082; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL808023; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC139231; AAI39232.1; -; mRNA.
DR EMBL; AK122479; BAC65761.1; -; mRNA.
DR CCDS; CCDS24989.1; -. [Q810B6-1]
DR PIR; T00253; T00253.
DR RefSeq; NP_033801.4; NM_009671.5. [Q810B6-1]
DR AlphaFoldDB; Q810B6; -.
DR SMR; Q810B6; -.
DR BioGRID; 198103; 34.
DR IntAct; Q810B6; 7.
DR MINT; Q810B6; -.
DR STRING; 10090.ENSMUSP00000118751; -.
DR iPTMnet; Q810B6; -.
DR PhosphoSitePlus; Q810B6; -.
DR EPD; Q810B6; -.
DR jPOST; Q810B6; -.
DR MaxQB; Q810B6; -.
DR PaxDb; Q810B6; -.
DR PeptideAtlas; Q810B6; -.
DR PRIDE; Q810B6; -.
DR ProteomicsDB; 296229; -. [Q810B6-1]
DR ProteomicsDB; 296230; -. [Q810B6-2]
DR Antibodypedia; 5541; 92 antibodies from 20 providers.
DR DNASU; 11736; -.
DR Ensembl; ENSMUST00000127610; ENSMUSP00000118252; ENSMUSG00000020790. [Q810B6-2]
DR Ensembl; ENSMUST00000155998; ENSMUSP00000118751; ENSMUSG00000020790. [Q810B6-1]
DR GeneID; 11736; -.
DR KEGG; mmu:11736; -.
DR UCSC; uc007jzh.1; mouse. [Q810B6-1]
DR CTD; 51479; -.
DR MGI; MGI:1337008; Ankfy1.
DR VEuPathDB; HostDB:ENSMUSG00000020790; -.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG4591; Eukaryota.
DR GeneTree; ENSGT00940000156179; -.
DR HOGENOM; CLU_599335_0_0_1; -.
DR InParanoid; Q810B6; -.
DR OMA; GPEGCQQ; -.
DR OrthoDB; 1115202at2759; -.
DR PhylomeDB; Q810B6; -.
DR TreeFam; TF351263; -.
DR Reactome; R-MMU-9013405; RHOD GTPase cycle.
DR BioGRID-ORCS; 11736; 11 hits in 73 CRISPR screens.
DR ChiTaRS; Ankfy1; mouse.
DR PRO; PR:Q810B6; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q810B6; protein.
DR Bgee; ENSMUSG00000020790; Expressed in stroma of bone marrow and 264 other tissues.
DR Genevisible; Q810B6; MM.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0044354; C:macropinosome; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0030904; C:retromer complex; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0006897; P:endocytosis; NAS:UniProtKB.
DR GO; GO:0016197; P:endosomal transport; ISO:MGI.
DR GO; GO:0034058; P:endosomal vesicle fusion; ISO:MGI.
DR GO; GO:0090160; P:Golgi to lysosome transport; ISO:MGI.
DR GO; GO:0048549; P:positive regulation of pinocytosis; ISO:MGI.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISO:MGI.
DR Gene3D; 1.25.40.20; -; 5.
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; 4.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF01363; FYVE; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 20.
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; 11.
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 Cytoplasmic vesicle; Endocytosis; Endosome; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9P2R3"
FT CHAIN 2..1169
FT /note="Rabankyrin-5"
FT /id="PRO_0000066891"
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:0000250|UniProtKB:Q9P2R3"
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:0000250|UniProtKB:Q9P2R3"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2R3"
FT VAR_SEQ 392..439
FT /note="LDLELKDHEGSTALWLAVQYITVSSDQSVNPFEDLPVVNGTSFDENSF ->
FT YVGRPGEMQSGCEGGIIRFRAERSRRQHCTLAGRPVHHCVFRPVCKPL (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:10092534, ECO:0000303|Ref.2"
FT /id="VSP_007917"
FT VAR_SEQ 440..1169
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10092534, ECO:0000303|Ref.2"
FT /id="VSP_007918"
FT CONFLICT 117..118
FT /note="ML -> IV (in Ref. 1; BAA24980 and 2; BAC67211/
FT BAC67388/BAC67389)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="F -> L (in Ref. 2; BAC67211)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="S -> T (in Ref. 2; BAC67389)"
FT /evidence="ECO:0000305"
FT CONFLICT 502
FT /note="G -> V (in Ref. 2; BAC67389)"
FT /evidence="ECO:0000305"
FT CONFLICT 526..527
FT /note="PV -> TL (in Ref. 2; BAC67211)"
FT /evidence="ECO:0000305"
FT CONFLICT 526
FT /note="P -> T (in Ref. 2; BAC67389)"
FT /evidence="ECO:0000305"
FT CONFLICT 840
FT /note="P -> S (in Ref. 2; BAC67389)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1169 AA; 128653 MW; AAFBB2D66739CA2F CRC64;
MAEEEVAKLE KHLMLLRQEY VKLQKKLAET EKRCTLLAAQ ANKENSNESF ISRLLAIVAG
LYEQEQYSDL KIKVGDRHIS AHKFVLAARS DSWSLANLSS TEEIDLSDAN PEVTMTMLRW
IYTDELEFRE DDVFLTELMK LANRFQLQLL RERCEKGVMS LVNVRNCIRF YQTAEELNAS
TLMNYCAEII ASHWDDLRKE DFSSLSAQLL YKMIKSKTEY PLHKAIKVER EDVVFLYLIE
MDSQLPGKLN ETDHNGDLAL DLALSRRLES IATTLVSHKA DVDMVDKNGW SLLHKGIQRG
DLFASTFLIK NGALVNAATA GAQETPLHLV ALYSPKKYSA DVMSEMAQIA EALLQAGANP
NMQDSKGRTP LHLSIMARND CVFSQLLQCK QLDLELKDHE GSTALWLAVQ YITVSSDQSV
NPFEDLPVVN GTSFDENSFA ARLIQRGSNT DAPDVMTGNC LLQRAAGAGN EAAALFLATS
GAHANHRNKW GETPLHTACR HGLANLTAEL LQQGANPNLQ TEEALPVPKE SPVLMSSADS
IYLQTPLHMA IAYNHPDVVS VILEQKANAL HATNNLQIIP DFSLKDSRDQ TVLGLALWTG
MHTIAAQLLG SGASINDTMS DGQTLLHMAI QRQDSKSALF LLEHQADINV RTQDGETALQ
LAIKHQLPLV VDAICTRGAD MSVPDEKGNP PLWLALASNL EDIASTLVRH GCDATCWGPG
PSGCLQTLLH RAVDENNEST ACFLIRSGCD VNSPRQPGTN GEGEEEARDG QTPLHLAASW
GLEETVQCLL EFGANVNAQD AEGRTPVHVA ISNQHSVIIQ LLISHPNIEL SVRDRQGLTP
FACAMTYKNN KAAEAILKRE SGAAEQVDNK GRNFLHVAVQ NSDIESVLFL ISVQANVNSR
VQDASKLTPL HLAVQAGSEI IVRNLLLAGA KVNELTKHRQ TALHLAAQQD LPTICSVLLE
NGVDFAAVDE NGNNALHLAV MHGRLNNIRA LLTECTVDAE AFNLRGQSPL HILGQYGKEN
AAAIFDLFLE CMPEYPLDKP DAEGNTVLLL AYMKGNANLC RAIVRSGVRL GVNNNQGVNI
FNYQVATKQL LFRLLDMLSK EPPWCDGSNC YECTAKFGVT TRKHHCRHCG RLLCHKCSTK
EIPIIKFDLN KPVRVCNICF DVLTLGGVS
