RETR3_XENTR
ID RETR3_XENTR Reviewed; 457 AA.
AC Q0P4Z1; Q07G99;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Reticulophagy regulator 3;
GN Name=retreg3; Synonyms=fam134c; ORFNames=TNeu105l15.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Neurula;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Interacts with ATG8 family modifier proteins.
CC {ECO:0000250|UniProtKB:Q86VR2}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DOMAIN: The LIR motif interacts with ATG8 family proteins.
CC {ECO:0000250|UniProtKB:Q86VR2}.
CC -!- SIMILARITY: Belongs to the RETREG family. {ECO:0000305}.
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DR EMBL; CR760241; CAL49403.1; -; mRNA.
DR EMBL; BC121834; AAI21835.1; -; mRNA.
DR RefSeq; NP_001016672.2; NM_001016672.3.
DR RefSeq; XP_012809972.1; XM_012954518.2.
DR AlphaFoldDB; Q0P4Z1; -.
DR PaxDb; Q0P4Z1; -.
DR DNASU; 549426; -.
DR GeneID; 549426; -.
DR KEGG; xtr:549426; -.
DR CTD; 162427; -.
DR Xenbase; XB-GENE-5719860; retreg3.
DR eggNOG; ENOG502QPTN; Eukaryota.
DR InParanoid; Q0P4Z1; -.
DR OrthoDB; 901531at2759; -.
DR Proteomes; UP000008143; Chromosome 10.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000014893; Expressed in skeletal muscle tissue and 14 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IEA:InterPro.
DR GO; GO:0061709; P:reticulophagy; IEA:InterPro.
DR InterPro; IPR043384; RETREG1/3.
DR InterPro; IPR033361; RETREG3.
DR PANTHER; PTHR28659; PTHR28659; 1.
DR PANTHER; PTHR28659:SF1; PTHR28659:SF1; 1.
PE 2: Evidence at transcript level;
KW Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..457
FT /note="Reticulophagy regulator 3"
FT /id="PRO_0000288471"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 435..440
FT /note="LIR motif"
FT /evidence="ECO:0000250|UniProtKB:Q9H6L5"
FT COMPBIAS 10..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 421
FT /note="Q -> R (in Ref. 1; CAL49403)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 457 AA; 51364 MW; 1351C6D711AC2585 CRC64;
MAQRVGEEEQ GASGLRRRRS GARCVEARER DEQVREVQEM LQRGLSSYEP VLSYVQAVLV
WERPRHSALL HLALNAAFWF FALTSLRIIF LVAFGLMIII CADQWKNKLW PELGAARASE
LENESWGYVH PRLLSVPELC YHAADTWVSV YNFLRNLLLF KTENPGKFCL LACSFLTFLA
VLGGYIPGVV LSYLLLLFLL LWPLAIYHQL GRRIYQKLEP ALQRLDFSVR GYMMSKYKER
QKHNRALPPT DASDSEEELA AFCPSLDDSA VAKELTISDS EHSDAEVSFT ENGTFNLSRG
QTPLTEGSED LDRHSDPEES FARDLPDFPS INPDATGIED DDETSIGIPS TALHPQFSSR
QLYEEQESLD AELSLGGFPS TQNITENIAG FVTRGMIQLA LAGASQQTHA YAESPRAKQY
QRNSSSELDT DAEADDFELL DQSELSQMDP SSSHSHQ