ID ANR27_HUMAN Reviewed; 1050 AA.
AC Q96NW4; Q71MF5; Q86UC3; Q8ND80; Q9H0I4;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 27-MAR-2024, entry version 165.
DE RecName: Full=Ankyrin repeat domain-containing protein 27;
DE AltName: Full=VPS9 domain-containing protein;
GN Name=ANKRD27; ORFNames=PP12899;
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 [LARGE SCALE MRNA], AND VARIANTS GLY-657 AND ARG-761.
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
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 MRNA].
RC TISSUE=Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-175.
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 644-1050.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP FUNCTION, INTERACTION WITH RAB21 AND RAB5A, AND SUBCELLULAR LOCATION.
RX PubMed=16525121; DOI=10.1242/jcs.02810;
RA Zhang X., He X., Fu X.-Y., Chang Z.;
RT "Varp is a Rab21 guanine nucleotide exchange factor and regulates endosome
RT dynamics.";
RL J. Cell Sci. 119:1053-1062(2006).
RN [7]
RP FUNCTION, AND INTERACTION WITH RAB38 AND RAB21.
RX PubMed=18477474; DOI=10.1016/j.bbrc.2008.05.017;
RA Wang F., Zhang H., Zhang X., Wang Y., Ren F., Zhang X., Zhai Y., Chang Z.;
RT "Varp interacts with Rab38 and functions as its potential effector.";
RL Biochem. Biophys. Res. Commun. 372:162-167(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1023, AND IDENTIFICATION BY
RP 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 FUNCTION, INTERACTION WITH RAB21 AND VAMP7, AND SUBCELLULAR LOCATION.
RX PubMed=19745841; DOI=10.1038/embor.2009.186;
RA Burgo A., Sotirakis E., Simmler M.C., Verraes A., Chamot C., Simpson J.C.,
RA Lanzetti L., Proux-Gillardeaux V., Galli T.;
RT "Role of Varp, a Rab21 exchange factor and TI-VAMP/VAMP7 partner, in
RT neurite growth.";
RL EMBO Rep. 10:1117-1124(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP INTERACTION WITH RAB32.
RX PubMed=21808068; DOI=10.1074/jbc.m111.261115;
RA Nottingham R.M., Ganley I.G., Barr F.A., Lambright D.G., Pfeffer S.R.;
RT "RUTBC1 protein, a Rab9A effector that activates GTP hydrolysis by Rab32
RT and Rab33B proteins.";
RL J. Biol. Chem. 286:33213-33222(2011).
RN [12]
RP FUNCTION, AND INTERACTION WITH KIF5A; KIF5C AND GOLGA4.
RX PubMed=22705394; DOI=10.1016/j.devcel.2012.04.019;
RA Burgo A., Proux-Gillardeaux V., Sotirakis E., Bun P., Casano A.,
RA Verraes A., Liem R.K., Formstecher E., Coppey-Moisan M., Galli T.;
RT "A molecular network for the transport of the TI-VAMP/VAMP7 vesicles from
RT cell center to periphery.";
RL Dev. Cell 23:166-180(2012).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-962; SER-970 AND THR-1023,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [14]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 659-921 IN COMPLEX WITH VAMP7,
RP SUBUNIT, FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-679;
RP ASP-681; MET-684 AND TYR-687.
RX PubMed=23104059; DOI=10.1038/nsmb.2414;
RA Schafer I.B., Hesketh G.G., Bright N.A., Gray S.R., Pryor P.R., Evans P.R.,
RA Luzio J.P., Owen D.J.;
RT "The binding of Varp to VAMP7 traps VAMP7 in a closed, fusogenically
RT inactive conformation.";
RL Nat. Struct. Mol. Biol. 19:1300-1309(2012).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 450-640 IN COMPLEX WITH RAB32,
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH VPS29, AND MUTAGENESIS OF
RP HIS-432; LEU-434; GLN-509; LEU-513; LYS-546; TYR-550; HIS-712 AND LEU-714.
RX PubMed=24856514; DOI=10.1016/j.devcel.2014.04.010;
RA Hesketh G.G., Perez-Dorado I., Jackson L.P., Wartosch L., Schafer I.B.,
RA Gray S.R., McCoy A.J., Zeldin O.B., Garman E.F., Harbour M.E., Evans P.R.,
RA Seaman M.N., Luzio J.P., Owen D.J.;
RT "VARP is recruited on to endosomes by direct interaction with retromer,
RT where together they function in export to the cell surface.";
RL Dev. Cell 29:591-606(2014).
CC -!- FUNCTION: May be a guanine exchange factor (GEF) for Rab21, Rab32 and
CC Rab38 and regulate endosome dynamics (PubMed:16525121,
CC PubMed:18477474). May regulate the participation of VAMP7 in membrane
CC fusion events; in vitro inhibits VAMP7-mediated SNARE complex formation
CC by trapping VAMP7 in a closed, fusogenically inactive conformation
CC (PubMed:23104059). Involved in peripheral melanosomal distribution of
CC TYRP1 in melanocytes; the function, which probably is implicating
CC vesicle-trafficking, includes cooperation with Rab32, Rab38 and VAMP7
CC (By similarity). Involved in the regulation of neurite growth; the
CC function seems to require its GEF activity, probably towards Rab21, and
CC VAMP7 but not Rab32/38 (By similarity). Proposed to be involved in
CC Golgi sorting of VAMP7 and transport of VAMP7 vesicles to the cell
CC surface; the function seems to implicate kinesin heavy chain isoform 5
CC proteins, GOLGA4, RAB21 and MACF1 (PubMed:22705394). Required for the
CC colocalization of VAMP7 and Rab21, probably on TGN sites
CC (PubMed:19745841). Involved in GLUT1 endosome-to-plasma membrane
CC trafficking; the function is dependent of association with VPS29
CC (PubMed:24856514). Regulates the proper trafficking of melanogenic
CC enzymes TYR, TYRP1 and DCT/TYRP2 to melanosomes in melanocytes (By
CC similarity). {ECO:0000250|UniProtKB:Q3UMR0,
CC ECO:0000269|PubMed:23104059, ECO:0000269|PubMed:24856514,
CC ECO:0000305|PubMed:16525121, ECO:0000305|PubMed:18477474,
CC ECO:0000305|PubMed:22705394}.
CC -!- SUBUNIT: Interacts with RAB21 (GDP-bound form), VPS29, RAB32 (GTP-bound
CC form), RAB38 (GTP-bound form), VAMP7, KIF5A, KIF5C, GOLGA4. Interacts
CC with low affinity with RAB5. ANKRD27:RAB32 heterodimers can
CC homodimerize to form tetramers. Can interact with RAB38 or RAB32, VPS29
CC and VAMP7 simultaneously (PubMed:16525121, PubMed:18477474,
CC PubMed:19745841, PubMed:22705394, PubMed:23104059, PubMed:24856514,
CC PubMed:21808068). A decreased interaction with RAB32 seen in the
CC presence of SGSM2 (PubMed:21808068). {ECO:0000269|PubMed:16525121,
CC ECO:0000269|PubMed:18477474, ECO:0000269|PubMed:19745841,
CC ECO:0000269|PubMed:21808068, ECO:0000269|PubMed:22705394,
CC ECO:0000269|PubMed:23104059, ECO:0000269|PubMed:24856514}.
CC -!- INTERACTION:
CC Q96NW4; Q13439: GOLGA4; NbExp=2; IntAct=EBI-6125599, EBI-1037845;
CC Q96NW4; Q12840: KIF5A; NbExp=4; IntAct=EBI-6125599, EBI-713468;
CC Q96NW4; P33175: Kif5a; Xeno; NbExp=2; IntAct=EBI-6125599, EBI-349710;
CC Q96NW4; P70280: Vamp7; Xeno; NbExp=13; IntAct=EBI-6125599, EBI-6555653;
CC Q96NW4; Q9JHW5: Vamp7; Xeno; NbExp=4; IntAct=EBI-6125599, EBI-919936;
CC -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:16525121,
CC ECO:0000269|PubMed:24856514}. Late endosome
CC {ECO:0000269|PubMed:23104059}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:23104059}. Lysosome {ECO:0000269|PubMed:23104059}.
CC Cell membrane {ECO:0000269|PubMed:23104059}. Melanosome
CC {ECO:0000250|UniProtKB:Q3UMR0}. Note=Colocalizes with VAMP7 in
CC transport vesicles in the shaft of hippocampal neurons (By similarity).
CC {ECO:0000250|UniProtKB:Q3UMR0}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB70755.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL136784; CAB66718.1; -; mRNA.
DR EMBL; AK054561; BAB70755.1; ALT_INIT; mRNA.
DR EMBL; BC050529; AAH50529.1; -; mRNA.
DR EMBL; AF447882; AAQ04657.1; -; mRNA.
DR EMBL; AL834335; CAD39003.1; -; mRNA.
DR CCDS; CCDS32986.1; -.
DR RefSeq; NP_115515.2; NM_032139.2.
DR RefSeq; XP_006723475.1; XM_006723412.2.
DR PDB; 4B93; X-ray; 2.00 A; B=659-921.
DR PDB; 4CYM; X-ray; 2.80 A; D/E/F=450-640.
DR PDB; 4CZ2; X-ray; 2.97 A; D/E/F=450-640.
DR PDB; 6TL0; NMR; -; B=692-746.
DR PDBsum; 4B93; -.
DR PDBsum; 4CYM; -.
DR PDBsum; 4CZ2; -.
DR PDBsum; 6TL0; -.
DR AlphaFoldDB; Q96NW4; -.
DR SMR; Q96NW4; -.
DR BioGRID; 123874; 43.
DR DIP; DIP-57614N; -.
DR IntAct; Q96NW4; 24.
DR MINT; Q96NW4; -.
DR STRING; 9606.ENSP00000304292; -.
DR iPTMnet; Q96NW4; -.
DR PhosphoSitePlus; Q96NW4; -.
DR SwissPalm; Q96NW4; -.
DR BioMuta; ANKRD27; -.
DR DMDM; 125987706; -.
DR CPTAC; CPTAC-1175; -.
DR CPTAC; CPTAC-1198; -.
DR EPD; Q96NW4; -.
DR jPOST; Q96NW4; -.
DR MassIVE; Q96NW4; -.
DR MaxQB; Q96NW4; -.
DR PaxDb; 9606-ENSP00000304292; -.
DR PeptideAtlas; Q96NW4; -.
DR ProteomicsDB; 77566; -.
DR Pumba; Q96NW4; -.
DR Antibodypedia; 47942; 103 antibodies from 25 providers.
DR DNASU; 84079; -.
DR Ensembl; ENST00000306065.9; ENSP00000304292.3; ENSG00000105186.16.
DR GeneID; 84079; -.
DR KEGG; hsa:84079; -.
DR MANE-Select; ENST00000306065.9; ENSP00000304292.3; NM_032139.3; NP_115515.2.
DR UCSC; uc002ntn.2; human.
DR AGR; HGNC:25310; -.
DR CTD; 84079; -.
DR DisGeNET; 84079; -.
DR GeneCards; ANKRD27; -.
DR HGNC; HGNC:25310; ANKRD27.
DR HPA; ENSG00000105186; Low tissue specificity.
DR MIM; 618957; gene.
DR neXtProt; NX_Q96NW4; -.
DR OpenTargets; ENSG00000105186; -.
DR PharmGKB; PA134893411; -.
DR VEuPathDB; HostDB:ENSG00000105186; -.
DR eggNOG; KOG2319; Eukaryota.
DR GeneTree; ENSGT00940000157021; -.
DR HOGENOM; CLU_010760_0_1_1; -.
DR InParanoid; Q96NW4; -.
DR OMA; LCHPLCT; -.
DR OrthoDB; 1199183at2759; -.
DR PhylomeDB; Q96NW4; -.
DR TreeFam; TF351261; -.
DR PathwayCommons; Q96NW4; -.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; Q96NW4; -.
DR BioGRID-ORCS; 84079; 10 hits in 1154 CRISPR screens.
DR ChiTaRS; ANKRD27; human.
DR GeneWiki; ANKRD27; -.
DR GenomeRNAi; 84079; -.
DR Pharos; Q96NW4; Tbio.
DR PRO; PR:Q96NW4; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q96NW4; Protein.
DR Bgee; ENSG00000105186; Expressed in choroid plexus epithelium and 202 other cell types or tissues.
DR ExpressionAtlas; Q96NW4; baseline and differential.
DR Genevisible; Q96NW4; HS.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0030133; C:transport vesicle; IBA:GO_Central.
DR GO; GO:0097422; C:tubular endosome; IDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:MGI.
DR GO; GO:0031267; F:small GTPase binding; IDA:UniProtKB.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0045022; P:early endosome to late endosome transport; IDA:MGI.
DR GO; GO:0032456; P:endocytic recycling; IMP:UniProtKB.
DR GO; GO:0035646; P:endosome to melanosome transport; IEA:Ensembl.
DR GO; GO:0035544; P:negative regulation of SNARE complex assembly; IDA:UniProtKB.
DR GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IEA:Ensembl.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd22885; ANKRD27_zf1; 1.
DR CDD; cd22886; ANKRD27_zf2; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR Gene3D; 1.20.1050.80; VPS9 domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR003123; VPS9.
DR InterPro; IPR037191; VPS9_dom_sf.
DR PANTHER; PTHR24170; ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 27; 1.
DR PANTHER; PTHR24170:SF2; ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 27; 1.
DR Pfam; PF00023; Ank; 2.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF02204; VPS9; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 8.
DR SMART; SM00167; VPS9; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 2.
DR SUPFAM; SSF109993; VPS9 domain; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 8.
DR PROSITE; PS51205; VPS9; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ANK repeat; Cell membrane; Cytoplasmic vesicle; Endosome;
KW GTPase activation; Guanine-nucleotide releasing factor; Lysosome; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..1050
FT /note="Ankyrin repeat domain-containing protein 27"
FT /id="PRO_0000274556"
FT DOMAIN 233..371
FT /note="VPS9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00550"
FT REPEAT 396..426
FT /note="ANK 1"
FT REPEAT 462..491
FT /note="ANK 2"
FT REPEAT 495..524
FT /note="ANK 3"
FT REPEAT 528..560
FT /note="ANK 4"
FT REPEAT 564..593
FT /note="ANK 5"
FT REPEAT 597..627
FT /note="ANK 6"
FT REPEAT 668..698
FT /note="ANK 7"
FT REPEAT 743..772
FT /note="ANK 8"
FT REPEAT 776..805
FT /note="ANK 9"
FT REPEAT 809..838
FT /note="ANK 10"
FT REPEAT 842..871
FT /note="ANK 11"
FT REGION 1..372
FT /note="Sufficient for GEF activity towards RAB21"
FT /evidence="ECO:0000269|PubMed:16525121"
FT REGION 396..460
FT /note="Sufficient for interaction with VPS29"
FT /evidence="ECO:0000269|PubMed:24856514"
FT REGION 451..730
FT /note="Interaction with RAB32"
FT /evidence="ECO:0000250|UniProtKB:Q3UMR0"
FT REGION 451..600
FT /note="Interaction with RAB38"
FT /evidence="ECO:0000250|UniProtKB:Q3UMR0,
FT ECO:0000269|PubMed:18477474"
FT REGION 625..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..707
FT /note="Required for interaction with VAMP7"
FT /evidence="ECO:0000250|UniProtKB:Q3UMR0,
FT ECO:0000269|PubMed:19745841, ECO:0000269|PubMed:23104059"
FT REGION 692..746
FT /note="Sufficient for interaction with VPS29"
FT /evidence="ECO:0000269|PubMed:24856514"
FT REGION 987..1050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 962
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 970
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1023
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 657
FT /note="S -> G (in dbSNP:rs2287669)"
FT /evidence="ECO:0000269|PubMed:11230166"
FT /id="VAR_030317"
FT VARIANT 761
FT /note="P -> R (in dbSNP:rs2302970)"
FT /evidence="ECO:0000269|PubMed:11230166"
FT /id="VAR_030318"
FT MUTAGEN 432
FT /note="H->A: Disrupts interaction with VPS29; when
FT associated with A-434."
FT /evidence="ECO:0000269|PubMed:24856514"
FT MUTAGEN 434
FT /note="L->A: Disrupts interaction with VPS29; when
FT associated with A-432."
FT /evidence="ECO:0000269|PubMed:24856514"
FT MUTAGEN 509
FT /note="Q->A: Disrupts interaction with RAB32."
FT /evidence="ECO:0000269|PubMed:24856514"
FT MUTAGEN 513
FT /note="L->D: Disrupts interaction with RAB32."
FT /evidence="ECO:0000269|PubMed:24856514"
FT MUTAGEN 546
FT /note="K->D: Impairs interaction with RAB32."
FT /evidence="ECO:0000269|PubMed:24856514"
FT MUTAGEN 550
FT /note="Y->A: Impairs interaction with RAB32."
FT /evidence="ECO:0000269|PubMed:24856514"
FT MUTAGEN 679
FT /note="D->A: Disrupts interaction with VAMP7."
FT /evidence="ECO:0000269|PubMed:23104059"
FT MUTAGEN 681
FT /note="D->A: Disrupts interaction with VAMP7."
FT /evidence="ECO:0000269|PubMed:23104059"
FT MUTAGEN 684
FT /note="M->D: Disrupts interaction with VAMP7."
FT /evidence="ECO:0000269|PubMed:23104059"
FT MUTAGEN 687
FT /note="Y->S: Disrupts interaction with VAMP7."
FT /evidence="ECO:0000269|PubMed:23104059"
FT MUTAGEN 712
FT /note="H->A: Disrupts interaction with VPS29; when
FT associated with A-714."
FT /evidence="ECO:0000269|PubMed:24856514"
FT MUTAGEN 714
FT /note="L->A: Disrupts interaction with VPS29; when
FT associated with A-712."
FT /evidence="ECO:0000269|PubMed:24856514"
FT CONFLICT 160..175
FT /note="HRTFRECERKSLRHHI -> LIEHSENARERASVTT (in Ref. 4;
FT AAQ04657)"
FT /evidence="ECO:0000305"
FT HELIX 466..473
FT /evidence="ECO:0007829|PDB:4CYM"
FT HELIX 476..484
FT /evidence="ECO:0007829|PDB:4CYM"
FT HELIX 499..506
FT /evidence="ECO:0007829|PDB:4CYM"
FT HELIX 509..517
FT /evidence="ECO:0007829|PDB:4CYM"
FT HELIX 532..538
FT /evidence="ECO:0007829|PDB:4CYM"
FT HELIX 542..551
FT /evidence="ECO:0007829|PDB:4CYM"
FT STRAND 552..554
FT /evidence="ECO:0007829|PDB:4CYM"
FT HELIX 568..574
FT /evidence="ECO:0007829|PDB:4CYM"
FT HELIX 578..586
FT /evidence="ECO:0007829|PDB:4CYM"
FT HELIX 601..604
FT /evidence="ECO:0007829|PDB:4CYM"
FT HELIX 608..615
FT /evidence="ECO:0007829|PDB:4CYM"
FT HELIX 668..678
FT /evidence="ECO:0007829|PDB:4B93"
FT HELIX 682..689
FT /evidence="ECO:0007829|PDB:4B93"
FT STRAND 734..736
FT /evidence="ECO:0007829|PDB:6TL0"
FT TURN 744..746
FT /evidence="ECO:0007829|PDB:6TL0"
FT HELIX 747..753
FT /evidence="ECO:0007829|PDB:4B93"
FT HELIX 759..765
FT /evidence="ECO:0007829|PDB:4B93"
FT HELIX 780..787
FT /evidence="ECO:0007829|PDB:4B93"
FT HELIX 790..798
FT /evidence="ECO:0007829|PDB:4B93"
FT HELIX 813..819
FT /evidence="ECO:0007829|PDB:4B93"
FT HELIX 823..825
FT /evidence="ECO:0007829|PDB:4B93"
FT HELIX 826..831
FT /evidence="ECO:0007829|PDB:4B93"
FT HELIX 846..852
FT /evidence="ECO:0007829|PDB:4B93"
FT HELIX 856..864
FT /evidence="ECO:0007829|PDB:4B93"
FT HELIX 880..882
FT /evidence="ECO:0007829|PDB:4B93"
FT HELIX 888..892
FT /evidence="ECO:0007829|PDB:4B93"
SQ SEQUENCE 1050 AA; 116984 MW; C47A96AA15E420F9 CRC64;
MALYDEDLLK NPFYLALQKC RPDLCSKVAQ IHGIVLVPCK GSLSSSIQST CQFESYILIP
VEEHFQTLNG KDVFIQGNRI KLGAGFACLL SVPILFEETF YNEKEESFSI LCIAHPLEKR
ESSEEPLAPS DPFSLKTIED VREFLGRHSE RFDRNIASFH RTFRECERKS LRHHIDSANA
LYTKCLQQLL RDSHLKMLAK QEAQMNLMKQ AVEIYVHHEI YNLIFKYVGT MEASEDAAFN
KITRSLQDLQ QKDIGVKPEF SFNIPRAKRE LAQLNKCTSP QQKLVCLRKV VQLITQSPSQ
RVNLETMCAD DLLSVLLYLL VKTEIPNWMA NLSYIKNFRF SSLAKDELGY CLTSFEAAIE
YIRQGSLSAK PPESEGFGDR LFLKQRMSLL SQMTSSPTDC LFKHIASGNQ KEVERLLSQE
DHDKDTVQKM CHPLCFCDDC EKLVSGRLND PSVVTPFSRD DRGHTPLHVA AVCGQASLID
LLVSKGAMVN ATDYHGATPL HLACQKGYQS VTLLLLHYKA SAEVQDNNGN TPLHLACTYG
HEDCVKALVY YDVESCRLDI GNEKGDTPLH IAARWGYQGV IETLLQNGAS TEIQNRLKET
PLKCALNSKI LSVMEAYHLS FERRQKSSEA PVQSPQRSVD SISQESSTSS FSSMSASSRQ
EETKKDYREV EKLLRAVADG DLEMVRYLLE WTEEDLEDAE DTVSAADPEF CHPLCQCPKC
APAQKRLAKV PASGLGVNVT SQDGSSPLHV AALHGRADLI PLLLKHGANA GARNADQAVP
LHLACQQGHF QVVKCLLDSN AKPNKKDLSG NTPLIYACSG GHHELVALLL QHGASINASN
NKGNTALHEA VIEKHVFVVE LLLLHGASVQ VLNKRQRTAV DCAEQNSKIM ELLQVVPSCV
ASLDDVAETD RKEYVTVKIR KKWNSKLYDL PDEPFTRQFY FVHSAGQFKG KTSREIMARD
RSVPNLTEGS LHEPGRQSVT LRQNNLPAQS GSHAAEKGNS DWPERPGLTQ TGPGHRRMLR
RHTVEDAVVS QGPEAAGPLS TPQEVSASRS
//
