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ANR27_PONAB
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   25-MAY-2022, entry version 77.
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   PRIDE; Q5REW9; -.
DR   GeneID; 100171616; -.
DR   KEGG; pon:100171616; -.
DR   CTD; 84079; -.
DR   InParanoid; Q5REW9; -.
DR   OrthoDB; 871322at2759; -.
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   Gene3D; 1.20.1050.80; -; 1.
DR   Gene3D; 1.25.40.20; -; 2.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR003123; VPS9.
DR   InterPro; IPR037191; VPS9_dom_sf.
DR   Pfam; PF00023; Ank; 1.
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; SSF109993; SSF109993; 1.
DR   SUPFAM; SSF48403; SSF48403; 2.
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
 
 
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