ID ANR27_PONAB Reviewed; 1050 AA.
AC Q5REW9;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 24-JAN-2024, entry version 82.
DE RecName: Full=Ankyrin repeat domain-containing protein 27;
GN Name=ANKRD27;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be a guanine exchange factor (GEF) for Rab21, Rab32 and
CC Rab38 and regulate endosome dynamics. May regulate the participation of
CC VAMP7 in membrane fusion events; in vitro inhibits VAMP7-mediated SNARE
CC complex formation by trapping VAMP7 in a closed, fusogenically inactive
CC conformation (By similarity). Involved in peripheral melanosomal
CC distribution of TYRP1 in melanocytes; the function, which probably is
CC implicating vesicle-trafficking, includes cooperation with Rab32, Rab38
CC and VAMP7. Involved in the regulation of neurite growth; the function
CC seems to require its GEF activity, probably towards Rab21, and VAMP7
CC but not Rab32/38. Proposed to be involved in Golgi sorting of VAMP7 and
CC transport of VAMP7 vesicles to the cell surface; the function seems to
CC implicate kinesin heavy chain isoform 5 proteins, GOLGA4, RAB21 and
CC MACF1. Required for the colocalization of VAMP7 and Rab21, probably on
CC TGN sites. Involved in GLUT1 endosome-to-plasma membrane trafficking;
CC the function is dependent of association with VPS29. Regulates the
CC proper trafficking of melanogenic enzymes TYR, TYRP1 and DCT/TYRP2 to
CC melanosomes in melanocytes (By similarity).
CC {ECO:0000250|UniProtKB:Q3UMR0, ECO:0000250|UniProtKB:Q96NW4}.
CC -!- SUBUNIT: Interacts with RAB21 (GDP-bound form), VPS29, KIF5A, KIF5C,
CC GOLGA4. Interacts with RAB32 (GTP-bound form), RAB38 (GTP-bound form),
CC VAMP7. Interacts with low affinity with RAB5. ANKRD27:RAB32
CC heterodimers can homodimerize to form tetramers. Can interact with
CC RAB38 or RAB32, VPS29 and VAMP7 simultaneously (By similarity). A
CC decreased interaction with RAB32 seen in the presence of SGSM2 (By
CC similarity). {ECO:0000250|UniProtKB:Q96NW4}.
CC -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000250|UniProtKB:Q96NW4}.
CC Late endosome {ECO:0000250|UniProtKB:Q96NW4}. Cytoplasmic vesicle
CC membrane {ECO:0000250|UniProtKB:Q96NW4}. Lysosome
CC {ECO:0000250|UniProtKB:Q96NW4}. Cell membrane
CC {ECO:0000250|UniProtKB:Q96NW4}. 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}.
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DR EMBL; CR857395; CAH89688.1; -; mRNA.
DR RefSeq; NP_001124765.1; NM_001131293.1.
DR AlphaFoldDB; Q5REW9; -.
DR SMR; Q5REW9; -.
DR STRING; 9601.ENSPPYP00000010994; -.
DR GeneID; 100171616; -.
DR KEGG; pon:100171616; -.
DR CTD; 84079; -.
DR InParanoid; Q5REW9; -.
DR OrthoDB; 1199183at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13637; Ank_4; 1.
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 2: Evidence at transcript level;
KW ANK repeat; Cell membrane; Cytoplasmic vesicle; Endosome; Lysosome;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW Transport.
FT CHAIN 1..1050
FT /note="Ankyrin repeat domain-containing protein 27"
FT /id="PRO_0000274558"
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:0000250|UniProtKB:Q96NW4"
FT REGION 396..460
FT /note="Sufficient for interaction with VPS29"
FT /evidence="ECO:0000250|UniProtKB:Q96NW4"
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:0000250|UniProtKB:Q96NW4"
FT REGION 630..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:0000250|UniProtKB:Q96NW4"
FT REGION 692..746
FT /note="Sufficient for interaction with VPS29"
FT /evidence="ECO:0000250|UniProtKB:Q96NW4"
FT REGION 987..1050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 962
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96NW4"
FT MOD_RES 970
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96NW4"
FT MOD_RES 1023
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96NW4"
SQ SEQUENCE 1050 AA; 117145 MW; 9736BF3085E1CD1D CRC64;
MALYDEDLLK NPFYLALQKW RPDLCSKVAQ IHGIVLVPCK GSLSSSIQST CQFESYILIP
VEEHFQTLNG KDVFIQGNRI KLGAGFTCLL SVPILFEETF YNEKEESFSI LCIAHPLEKR
ESSEEPLAPS DPFSLKTIED VREFLGRHSE RFDRNIASFH RTFRECERKS LRHHIDSANA
LYTKCLQQLL RDSHLKMLAK QEAQMNLMKQ AVEIYVHHEI YDLIFKYVGT MEASEDAAFN
KITRSLQDLQ QKDIGVKPEF SFNIPRAKRE LAQLNKCTSP QQKLVCLRKV VQLITQSPSQ
RVNLETMCAD DLLSVLLYLL VKTEIPNWMA NLSYIKNFRF SSSAKDELGY CLTSFEAAIE
YIRQGSLSAK PPESEGFGDR LFLKQRMSLL SQMTSSPTDC LFKHIASGNQ KEVERLLSQE
DHDKDAVQKM CHPLCFCDDC EKLVSGRLND PSVVTPFSRD DRGHTPLHVA ALCGQASLID
LLVSKGAVVN ATDYHGATPL HLACQKGYQS VTLLLLHYKA SAEVQDNNGN TPLHLACTYG
HEDCVKALVY YDVESCRLDI GNEKGDTPLH IAARWGYQAI IETLLQNGAS PEIQNRLKET
PLKCALNSKI LSVMEAYHLS FERRQKSSEA PVQSLQRSVD SISQESSTSS FSSMSAGSRQ
EETKKDYREV EKLLRAVADG DLEMVRYLLE WTEEDLEDAE DTVSAVDPEF CHPLCQCPKC
APAQKRLAKV PASGLGVNVT SQDGSSPLYV AALHGRADLI PLLLKHGANA GARNADQAVP
LHLACQQGHF QVVKCLLDSN AKPNKKDLSG NTPLIYACSG GHHEVVALLL QHGAAINTSN
NKGNTALHEA VIEKHVFVVE LLLLHGASVQ VLNKRQRTAV DCAEQNSKIM ELLQVVPSCV
ASLDDVAETD RKEYVTVKIR KKWNSKLYDL PDEPFTRQFY FAHSAGQFKG KTSREIMARD
RSVPNLTEGS LHEPGRQSVT LRQNNLPAQS GSHAAEKGNS DWPERPRVTQ TGPGHRRMLR
RHTVEDAVVS QGPEAAGPLS TPQEVSASRS
//
