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RETR1_BOVIN
ID   RETR1_BOVIN             Reviewed;         493 AA.
AC   Q5E9K8; A5PJF3;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 2.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Reticulophagy regulator 1;
DE   AltName: Full=Reticulophagy receptor 1 {ECO:0000305};
GN   Name=RETREG1; Synonyms=FAM134B;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=Crossbred X Angus, and Hereford; TISSUE=Hypothalamus, and Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Endoplasmic reticulum-anchored autophagy receptor that
CC       mediates ER delivery into lysosomes through sequestration into
CC       autophagosomes. Promotes membrane remodeling and ER scission via its
CC       membrane bending capacity and targets the fragments into autophagosomes
CC       via interaction with ATG8 family proteins. Required for long-term
CC       survival of nociceptive and autonomic ganglion neurons.
CC       {ECO:0000250|UniProtKB:Q9H6L5}.
CC   -!- SUBUNIT: Interacts with ATG8 family modifier proteins MAP1LC3A,
CC       MAP1LC3B, GABARAP, GABARAPL1 and GABARAPL2.
CC       {ECO:0000250|UniProtKB:Q9H6L5}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane
CC       {ECO:0000250|UniProtKB:Q8VE91}; Multi-pass membrane protein
CC       {ECO:0000255}. Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q9H6L5}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5E9K8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5E9K8-2; Sequence=VSP_057835;
CC   -!- DOMAIN: The LIR motif interacts with ATG8 family proteins and is
CC       necessary to target the ER fragments to autophagosomes for lysosomal
CC       degradation. {ECO:0000250|UniProtKB:Q9H6L5}.
CC   -!- DOMAIN: The reticulon homology domain provides capacity to bend the
CC       membrane and promotes ER scission (By similarity). This domain does not
CC       show relevant similarities with reticulon domains, preventing any
CC       domain predictions within the protein sequence.
CC       {ECO:0000250|UniProtKB:Q9H6L5, ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the RETREG family. {ECO:0000305}.
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DR   EMBL; BT020912; AAX08929.1; -; mRNA.
DR   EMBL; BC102079; AAI02080.1; -; mRNA.
DR   EMBL; BC142089; AAI42090.1; -; mRNA.
DR   RefSeq; NP_001015672.1; NM_001015672.2. [Q5E9K8-2]
DR   AlphaFoldDB; Q5E9K8; -.
DR   STRING; 9913.ENSBTAP00000021862; -.
DR   PaxDb; Q5E9K8; -.
DR   Ensembl; ENSBTAT00000021862; ENSBTAP00000021862; ENSBTAG00000016444. [Q5E9K8-2]
DR   GeneID; 540068; -.
DR   KEGG; bta:540068; -.
DR   CTD; 54463; -.
DR   VEuPathDB; HostDB:ENSBTAG00000016444; -.
DR   eggNOG; ENOG502QPW8; Eukaryota.
DR   GeneTree; ENSGT00940000160746; -.
DR   InParanoid; Q5E9K8; -.
DR   OrthoDB; 901531at2759; -.
DR   TreeFam; TF329111; -.
DR   Proteomes; UP000009136; Chromosome 20.
DR   Bgee; ENSBTAG00000016444; Expressed in gluteal muscle and 108 other tissues.
DR   ExpressionAtlas; Q5E9K8; baseline and differential.
DR   GO; GO:0005801; C:cis-Golgi network; ISS:UniProtKB.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:GO_Central.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:GO_Central.
DR   GO; GO:0061709; P:reticulophagy; ISS:GO_Central.
DR   GO; GO:0019233; P:sensory perception of pain; ISS:UniProtKB.
DR   InterPro; IPR033358; RETREG1.
DR   InterPro; IPR043384; RETREG1/3.
DR   PANTHER; PTHR28659; PTHR28659; 1.
DR   PANTHER; PTHR28659:SF3; PTHR28659:SF3; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Autophagy; Endoplasmic reticulum; Golgi apparatus;
KW   Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..493
FT                   /note="Reticulophagy regulator 1"
FT                   /id="PRO_0000288465"
FT   TOPO_DOM        1..55
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6L5"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        77..87
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        109..114
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        115..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        136..204
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        205..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        226..493
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6L5"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          80..229
FT                   /note="Reticulon homology domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6L5"
FT   REGION          315..394
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          435..493
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           449..454
FT                   /note="LIR motif"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6L5"
FT   COMPBIAS        19..38
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..360
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        363..384
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        442..459
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        462..486
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         353
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VE91"
FT   VAR_SEQ         1..148
FT                   /note="MASPAPPEPAEQGSPALAAAPQAPPPPTRAPPEEPEGAAPPEEGAAAGAGRQ
FT                   VEEAAGGVAAVVTWLLGEPALWLGGRADELLSWKRPLHSLLAFVGANLVFWFLALTPWR
FT                   VYHLISVMILTRVIMQIIKDMILSRTRGAQLWRSLSE -> MPEGEDFGPGK (in
FT                   isoform 2)"
FT                   /id="VSP_057835"
SQ   SEQUENCE   493 AA;  53680 MW;  3FD62FAF32342A05 CRC64;
     MASPAPPEPA EQGSPALAAA PQAPPPPTRA PPEEPEGAAP PEEGAAAGAG RQVEEAAGGV
     AAVVTWLLGE PALWLGGRAD ELLSWKRPLH SLLAFVGANL VFWFLALTPW RVYHLISVMI
     LTRVIMQIIK DMILSRTRGA QLWRSLSESW EVINSKPDER PGFSHCLAES WMNFSIFLQE
     MSVFKQQSPG KFCLLVCSVC TFFTILGSYI PGVILSYLLL LCAFLCPLFK CNDIGQKIYS
     KIKSCLLKLD FGIREYINQK KRERSEADKE KSHKDDSELD FSALCPKISL TTAAKELSVS
     DTDVSEVSWT DNGTFNLSEG YTPQTDTSDD LDRPSEEVFS RDLSDFPSLE NGTGTNDEDE
     LSLGLPTELK RKKEQLDGGP RRSTEKKSAA GLSLPLSSDQ TLHLMSDLAG DVITAAVTAA
     VKDQLAGVRQ ALSQAAPSLG EDTDTEEGDD FELLDQSELD QIESELGLSQ DQEAEAQQNK
     KSSGFLSNLL GGH
 
 
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