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Rabankyrin-5 (Rank-5) (Ankyrin repeat and FYVE domain-containing protein 1) (Ankyrin repeats hooked to a zinc finger motif)

 ANFY1_MOUSE             Reviewed;        1169 AA.
Q810B6; B1ATS3; O54807; Q80TG6; Q80UH8;
04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
25-APR-2018, entry version 135.
RecName: Full=Rabankyrin-5 {ECO:0000303|PubMed:15328530};
Short=Rank-5;
AltName: Full=Ankyrin repeat and FYVE domain-containing protein 1;
AltName: Full=Ankyrin repeats hooked to a zinc finger motif;
Name=Ankfy1; Synonyms=Ankhzn, Kiaa1255;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND SUBCELLULAR LOCATION.
PubMed=10092534; DOI=10.1006/bbrc.1999.0430;
Ito K., Ishii N., Miyashita A., Tominaga K., Kuriyama H., Maruyama H.,
Shirai M., Naito M., Arakawa M., Kuwano R.;
"Molecular cloning of a novel 130-kDa cytoplasmic protein, Ankhzn,
containing ankyrin repeats hooked to a zinc finger motif.";
Biochem. Biophys. Res. Commun. 257:206-213(1999).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), AND
SEQUENCE REVISION.
Maruyama H., Kuriyama H., Ishii N., Ito K., Odani S., Kuwano R.;
"Genomic organization, alternative splicing, and promoter assay of the
mouse Ankhzn gene.";
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 994-1169 (ISOFORM 1).
TISSUE=Brain;
PubMed=12693553; DOI=10.1093/dnares/10.1.35;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
Nakajima D., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
II. The complete nucleotide sequences of 400 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:35-48(2003).
[6]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15328530; DOI=10.1371/journal.pbio.0020261;
Schnatwinkel C., Christoforidis S., Lindsay M.R.,
Uttenweiler-Joseph S., Wilm M., Parton R.G., Zerial M.;
"The Rab5 effector Rabankyrin-5 regulates and coordinates different
endocytic mechanisms.";
PLoS Biol. 2:E261-E261(2004).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Proposed effector of Rab5. Binds to phosphatidylinositol
3-phosphate (PI(3)P). Involved in homotypic early endosome fusion
and to a lesser extent in heterotypic fusion of chlathrin-coated
vesicles with early endosomes. Required for correct endosomal
localization. Involved in the internalization and trafficking of
activated tyrosine kinase receptors such as PDGFRB. Regulates the
subcellular localization of the retromer complex in a EHD1-
dependent manner. Involved in endosome-to-Golgi transport and
biosynthetic transport to late endosomes and lysosomes indicative
for a regulation of retromer complex-mediated retrograde transport
(By similarity). Involved in macropinocytosis; the function is
dependent on Rab5-GTP. {ECO:0000250|UniProtKB:Q9P2R3,
ECO:0000269|PubMed:15328530}.
-!- SUBUNIT: Interacts with RAB5A (in GTP-bound form). Interacts with
RHOD (independent of GTP-loaded status). Interacts with EHD1.
Interacts with VPS26A; the interaction is indepenedent of EHD1 and
is indicative for an association with the cargo recognition
subcomplex of the retromer complex.
{ECO:0000250|UniProtKB:Q9P2R3}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10092534}.
Endosome membrane {ECO:0000269|PubMed:10092534}; Peripheral
membrane protein {ECO:0000269|PubMed:10092534}. Cytoplasmic
vesicle {ECO:0000269|PubMed:15328530}. Note=Also associated with
endosomal membranes. Localizes to macropinosomes. In kidney
proximal tubule cells localizes to vesicle-like structures
underneath the apical brush border. {ECO:0000269|PubMed:15328530}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q810B6-1; Sequence=Displayed;
Name=2;
IsoId=Q810B6-2; Sequence=VSP_007917, VSP_007918;
-!- TISSUE SPECIFICITY: Expressed in kidney proximal tubule epithelial
cells; at protein level. {ECO:0000269|PubMed:15328530}.
-----------------------------------------------------------------------
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EMBL; AB011370; BAA24980.2; -; mRNA.
EMBL; AB098329; BAC67211.1; -; mRNA.
EMBL; AB098157; BAC67389.1; -; Genomic_DNA.
EMBL; AB098157; BAC67388.1; -; Genomic_DNA.
EMBL; AL663082; CAI25188.1; -; Genomic_DNA.
EMBL; AL808023; CAI25188.1; JOINED; Genomic_DNA.
EMBL; AL808023; CAI25205.1; -; Genomic_DNA.
EMBL; AL663082; CAI25205.1; JOINED; Genomic_DNA.
EMBL; BC139231; AAI39232.1; -; mRNA.
EMBL; AK122479; BAC65761.1; -; mRNA.
CCDS; CCDS24989.1; -. [Q810B6-1]
PIR; T00253; T00253.
RefSeq; NP_033801.4; NM_009671.5. [Q810B6-1]
UniGene; Mm.10313; -.
ProteinModelPortal; Q810B6; -.
SMR; Q810B6; -.
BioGrid; 198103; 8.
IntAct; Q810B6; 6.
STRING; 10090.ENSMUSP00000118751; -.
iPTMnet; Q810B6; -.
PhosphoSitePlus; Q810B6; -.
EPD; Q810B6; -.
PaxDb; Q810B6; -.
PeptideAtlas; Q810B6; -.
PRIDE; Q810B6; -.
Ensembl; ENSMUST00000127610; ENSMUSP00000118252; ENSMUSG00000020790. [Q810B6-2]
Ensembl; ENSMUST00000155998; ENSMUSP00000118751; ENSMUSG00000020790. [Q810B6-1]
GeneID; 11736; -.
KEGG; mmu:11736; -.
UCSC; uc007jzh.1; mouse. [Q810B6-1]
CTD; 51479; -.
MGI; MGI:1337008; Ankfy1.
eggNOG; KOG0504; Eukaryota.
eggNOG; KOG4591; Eukaryota.
eggNOG; COG0666; LUCA.
GeneTree; ENSGT00910000144044; -.
HOGENOM; HOG000022583; -.
HOVERGEN; HBG050501; -.
InParanoid; Q810B6; -.
KO; K20129; -.
OMA; MLRWIYT; -.
OrthoDB; EOG091G0ITN; -.
TreeFam; TF351263; -.
PRO; PR:Q810B6; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000020790; -.
CleanEx; MM_ANKFY1; -.
Genevisible; Q810B6; MM.
GO; GO:0005829; C:cytosol; IEA:GOC.
GO; GO:0005769; C:early endosome; ISO:MGI.
GO; GO:0005768; C:endosome; ISO:MGI.
GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0044354; C:macropinosome; ISO:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0030904; C:retromer complex; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:1901981; F:phosphatidylinositol phosphate binding; ISO:MGI.
GO; GO:0017137; F:Rab GTPase binding; ISO:MGI.
GO; GO:0006897; P:endocytosis; NAS:UniProtKB.
GO; GO:0034058; P:endosomal vesicle fusion; ISO:MGI.
GO; GO:0090160; P:Golgi to lysosome transport; ISO:MGI.
GO; GO:0048549; P:positive regulation of pinocytosis; ISO:MGI.
GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISO:MGI.
CDD; cd00204; ANK; 7.
Gene3D; 1.25.40.20; -; 6.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR000210; BTB/POZ_dom.
InterPro; IPR011333; SKP1/BTB/POZ_sf.
InterPro; IPR000306; Znf_FYVE.
InterPro; IPR017455; Znf_FYVE-rel.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF00023; Ank; 2.
Pfam; PF12796; Ank_2; 4.
Pfam; PF00651; BTB; 1.
Pfam; PF01363; FYVE; 1.
PRINTS; PR01415; ANKYRIN.
SMART; SM00248; ANK; 20.
SMART; SM00225; BTB; 1.
SMART; SM00064; FYVE; 1.
SUPFAM; SSF48403; SSF48403; 4.
SUPFAM; SSF54695; SSF54695; 1.
SUPFAM; SSF57903; SSF57903; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 11.
PROSITE; PS50097; BTB; 1.
PROSITE; PS50178; ZF_FYVE; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; ANK repeat; Complete proteome;
Cytoplasm; Cytoplasmic vesicle; Endocytosis; Endosome; Membrane;
Metal-binding; Phosphoprotein; Reference proteome; Repeat; Zinc;
Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q9P2R3}.
CHAIN 2 1169 Rabankyrin-5.
/FTId=PRO_0000066891.
DOMAIN 68 130 BTB. {ECO:0000255|PROSITE-
ProRule:PRU00037}.
REPEAT 217 247 ANK 1.
REPEAT 255 284 ANK 2.
REPEAT 288 317 ANK 3.
REPEAT 322 362 ANK 4.
REPEAT 366 396 ANK 5.
REPEAT 490 519 ANK 6.
REPEAT 542 572 ANK 7.
REPEAT 588 617 ANK 8.
REPEAT 621 650 ANK 9.
REPEAT 654 683 ANK 10.
REPEAT 687 716 ANK 11.
REPEAT 724 753 ANK 12.
REPEAT 769 798 ANK 13.
REPEAT 802 832 ANK 14.
REPEAT 836 865 ANK 15.
REPEAT 870 899 ANK 16.
REPEAT 905 934 ANK 17.
REPEAT 938 967 ANK 18.
REPEAT 971 1001 ANK 19.
REPEAT 1005 1037 ANK 20.
REPEAT 1043 1072 ANK 21.
ZN_FING 1104 1164 FYVE-type. {ECO:0000255|PROSITE-
ProRule:PRU00091}.
REGION 650 759 Interaction with RHOD and RAB5A.
{ECO:0000250|UniProtKB:Q9P2R3}.
MOTIF 421 423 NPF.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q9P2R3}.
MOD_RES 270 270 Phosphoserine.
{ECO:0000250|UniProtKB:Q9P2R3}.
VAR_SEQ 392 439 LDLELKDHEGSTALWLAVQYITVSSDQSVNPFEDLPVVNGT
SFDENSF -> YVGRPGEMQSGCEGGIIRFRAERSRRQHCT
LAGRPVHHCVFRPVCKPL (in isoform 2).
{ECO:0000303|PubMed:10092534,
ECO:0000303|Ref.2}.
/FTId=VSP_007917.
VAR_SEQ 440 1169 Missing (in isoform 2).
{ECO:0000303|PubMed:10092534,
ECO:0000303|Ref.2}.
/FTId=VSP_007918.
CONFLICT 117 118 ML -> IV (in Ref. 1; BAA24980 and 2;
BAC67211/BAC67388/BAC67389).
{ECO:0000305}.
CONFLICT 439 439 F -> L (in Ref. 2; BAC67211).
{ECO:0000305}.
CONFLICT 448 448 S -> T (in Ref. 2; BAC67389).
{ECO:0000305}.
CONFLICT 502 502 G -> V (in Ref. 2; BAC67389).
{ECO:0000305}.
CONFLICT 526 527 PV -> TL (in Ref. 2; BAC67211).
{ECO:0000305}.
CONFLICT 526 526 P -> T (in Ref. 2; BAC67389).
{ECO:0000305}.
CONFLICT 840 840 P -> S (in Ref. 2; BAC67389).
{ECO:0000305}.
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


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