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Database: UniProt
Entry: A0A1A6H8X7_NEOLE
LinkDB: A0A1A6H8X7_NEOLE
Original site: A0A1A6H8X7_NEOLE 
ID   A0A1A6H8X7_NEOLE        Unreviewed;       433 AA.
AC   A0A1A6H8X7;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Acyl-CoA-binding domain-containing protein 5 {ECO:0000256|ARBA:ARBA00018418};
GN   ORFNames=A6R68_15402 {ECO:0000313|EMBL:OBS74062.1};
OS   Neotoma lepida (Desert woodrat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Neotominae; Neotoma.
OX   NCBI_TaxID=56216 {ECO:0000313|EMBL:OBS74062.1, ECO:0000313|Proteomes:UP000092124};
RN   [1] {ECO:0000313|EMBL:OBS74062.1, ECO:0000313|Proteomes:UP000092124}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=417 {ECO:0000313|EMBL:OBS74062.1};
RC   TISSUE=Liver {ECO:0000313|EMBL:OBS74062.1};
RA   Campbell M., Oakeson K.F., Yandell M., Halpert J.R., Dearing D.;
RT   "The Draft Genome Sequence and Annotation of the Desert Woodrat Neotoma
RT   lepida.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acyl-CoA binding protein which acts as the peroxisome
CC       receptor for pexophagy but is dispensable for aggrephagy and
CC       nonselective autophagy. Binds medium- and long-chain acyl-CoA esters.
CC       {ECO:0000256|ARBA:ARBA00025481}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Peroxisome
CC       membrane {ECO:0000256|ARBA:ARBA00004549}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004549}.
CC   -!- SIMILARITY: Belongs to the ATG37 family.
CC       {ECO:0000256|ARBA:ARBA00010310}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OBS74062.1}.
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DR   EMBL; LZPO01044512; OBS74062.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1A6H8X7; -.
DR   STRING; 56216.A0A1A6H8X7; -.
DR   Proteomes; UP000092124; Unassembled WGS sequence.
DR   GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000062; F:fatty-acyl-CoA binding; IEA:InterPro.
DR   GO; GO:0030242; P:autophagy of peroxisome; IEA:InterPro.
DR   CDD; cd00435; ACBP; 1.
DR   Gene3D; 1.20.80.10; -; 1.
DR   InterPro; IPR016347; ACBD5.
DR   InterPro; IPR022408; Acyl-CoA-binding_prot_CS.
DR   InterPro; IPR000582; Acyl-CoA-binding_protein.
DR   InterPro; IPR035984; Acyl-CoA-binding_sf.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR   PANTHER; PTHR23310:SF6; ACYL-COA-BINDING DOMAIN-CONTAINING PROTEIN 5; 1.
DR   PANTHER; PTHR23310; ACYL-COA-BINDING PROTEIN, ACBP; 1.
DR   Pfam; PF00887; ACBP; 1.
DR   PIRSF; PIRSF002412; MA_DBI; 3.
DR   PRINTS; PR00689; ACOABINDINGP.
DR   SUPFAM; SSF47027; Acyl-CoA binding protein; 1.
DR   PROSITE; PS00880; ACB_1; 1.
DR   PROSITE; PS51228; ACB_2; 1.
PE   3: Inferred from homology;
KW   Autophagy {ECO:0000256|ARBA:ARBA00023006};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092124};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        405..425
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          81..170
FT                   /note="ACB"
FT                   /evidence="ECO:0000259|PROSITE:PS51228"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          194..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          302..358
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        218..241
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        302..334
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         92..101
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002412-1"
FT   BINDING         112..116
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002412-1"
FT   BINDING         138
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002412-1"
FT   BINDING         157
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002412-1"
SQ   SEQUENCE   433 AA;  48576 MW;  B68BF80CBF7F1DC8 CRC64;
     MTPAHRGRGP EAPGNYSSHK PAGQGEGQAS RHNRTGLAKS FGYYQGSWES WCCCCCLIPA
     DRPWDRGRRW QLEMADTRSV HETRFEAAVK VIQSLPKNGS FQPTNEMMLK FYSFYKQATE
     GPCKLSRPGF WDPIGRYKWD AWSSLGDMTK EEAMIAYVEE MKKILETMPM TEKVEELLHV
     IDLGNVLVSS NAKAVNGKTE SSDSGAESEE EEAQEEFKGA EQSDSNDRND DHSEDASGIH
     LTSDSDSEVY CDSMEQFGQE EYYLGGDPSQ HLENSGVCED AQISPGNGSI GKMRMVAVEG
     KGEVKRGGED GRSNSGAPHR EKRGGERHRM PHLSEGTQGR QVGSGGDGER WGSDRGSRGS
     LNEQIALVLI RLQEDMQNVL QRLHKLETLA ASQRPSWWPF EMSPGALTFA ILWPFIAQWL
     VHLYYQRRRR KLN
//
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