SEC13_BOVIN
ID SEC13_BOVIN Reviewed; 322 AA.
AC Q3ZCC9;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Protein SEC13 homolog {ECO:0000305};
DE AltName: Full=GATOR complex protein SEC13 {ECO:0000305};
DE AltName: Full=SEC13-like protein 1;
GN Name=SEC13; Synonyms=SEC13L1;
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].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Functions as a component of the nuclear pore complex (NPC)
CC and the COPII coat. At the endoplasmic reticulum, SEC13 is involved in
CC the biogenesis of COPII-coated vesicles. Required for the exit of
CC adipsin (CFD/ADN), an adipocyte-secreted protein from the endoplasmic
CC reticulum. {ECO:0000250|UniProtKB:P55735,
CC ECO:0000250|UniProtKB:Q9D1M0}.
CC -!- FUNCTION: As a component of the GATOR subcomplex GATOR2, functions
CC within the amino acid-sensing branch of the TORC1 signaling pathway.
CC Indirectly activates mTORC1 and the TORC1 signaling pathway through the
CC inhibition of the GATOR1 subcomplex. It is negatively regulated by the
CC upstream amino acid sensors SESN2 and CASTOR1.
CC {ECO:0000250|UniProtKB:P55735}.
CC -!- SUBUNIT: At the nuclear pore: component of the Y-shaped Nup107-160
CC subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex
CC includes NUP160, NUP133, NUP107, NUP98, NUP85, NUP43, NUP37, SEH1 and
CC SEC13. At the COPII coat complex: interacts with SEC31A and SEC31B.
CC Within the GATOR complex, component of the GATOR2 subcomplex, made of
CC MIOS, SEC13, SEH1L, WDR24 and WDR59. The GATOR complex strongly
CC interacts with RRAGA/RRAGC and RRAGB/RRAGC heterodimers. The GATOR2
CC complex interacts with CASTOR2 and CASTOR1; the interaction is
CC negatively regulated by arginine. The GATOR2 complex interacts with
CC SESN1, SESN2 and SESN3; the interaction is negatively regulated by
CC amino acids. Interacts with SEC16A. Interacts with SEC16B.
CC {ECO:0000250|UniProtKB:P55735}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC membrane {ECO:0000250|UniProtKB:P55735}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P55735}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P55735}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P55735}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P55735}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P55735}. Nucleus, nuclear pore complex
CC {ECO:0000250|UniProtKB:P55735}. Lysosome membrane
CC {ECO:0000250|UniProtKB:P55735}. Note=In interphase, localizes at both
CC sides of the NPC. {ECO:0000250|UniProtKB:P55735}.
CC -!- SIMILARITY: Belongs to the WD repeat SEC13 family. {ECO:0000305}.
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DR EMBL; BC102514; AAI02515.1; -; mRNA.
DR RefSeq; NP_001069033.1; NM_001075565.2.
DR AlphaFoldDB; Q3ZCC9; -.
DR SMR; Q3ZCC9; -.
DR STRING; 9913.ENSBTAP00000023702; -.
DR PaxDb; Q3ZCC9; -.
DR PeptideAtlas; Q3ZCC9; -.
DR PRIDE; Q3ZCC9; -.
DR Ensembl; ENSBTAT00000023702; ENSBTAP00000023702; ENSBTAG00000017825.
DR GeneID; 512530; -.
DR KEGG; bta:512530; -.
DR CTD; 6396; -.
DR VEuPathDB; HostDB:ENSBTAG00000017825; -.
DR VGNC; VGNC:34403; SEC13.
DR eggNOG; KOG1332; Eukaryota.
DR GeneTree; ENSGT00940000153393; -.
DR HOGENOM; CLU_032441_0_1_1; -.
DR InParanoid; Q3ZCC9; -.
DR OMA; TVDTGHE; -.
DR OrthoDB; 944756at2759; -.
DR TreeFam; TF300815; -.
DR Reactome; R-BTA-204005; COPII-mediated vesicle transport.
DR Reactome; R-BTA-2132295; MHC class II antigen presentation.
DR Reactome; R-BTA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR Proteomes; UP000009136; Chromosome 22.
DR Bgee; ENSBTAG00000017825; Expressed in saliva-secreting gland and 108 other tissues.
DR GO; GO:0030127; C:COPII vesicle coat; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0061700; C:GATOR2 complex; IEA:Ensembl.
DR GO; GO:0000776; C:kinetochore; IEA:Ensembl.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0031080; C:nuclear pore outer ring; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0005198; F:structural molecule activity; IBA:GO_Central.
DR GO; GO:0090114; P:COPII-coated vesicle budding; IBA:GO_Central.
DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; IEA:Ensembl.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0032008; P:positive regulation of TOR signaling; IBA:GO_Central.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IEA:InterPro.
DR GO; GO:0032527; P:protein exit from endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR037596; Sec13.
DR InterPro; IPR037363; Sec13/Seh1_fam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR11024; PTHR11024; 1.
DR PANTHER; PTHR11024:SF2; PTHR11024:SF2; 1.
DR Pfam; PF00400; WD40; 5.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasmic vesicle; Endoplasmic reticulum;
KW ER-Golgi transport; Lysosome; Membrane; mRNA transport;
KW Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Translocation; Transport; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P55735"
FT CHAIN 2..322
FT /note="Protein SEC13 homolog"
FT /id="PRO_0000281769"
FT REPEAT 11..50
FT /note="WD 1"
FT REPEAT 55..96
FT /note="WD 2"
FT REPEAT 101..144
FT /note="WD 3"
FT REPEAT 148..204
FT /note="WD 4"
FT REPEAT 210..253
FT /note="WD 5"
FT REPEAT 260..299
FT /note="WD 6"
FT MOD_RES 2
FT /note="N-acetylvaline"
FT /evidence="ECO:0000250|UniProtKB:P55735"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55735"
SQ SEQUENCE 322 AA; 35472 MW; 551BAC942D2965CF CRC64;
MVSVINTVDT SHEDMIHDAQ MDYYGTRLAT CSSDRSVKIF DVRNGGQILV ADLRGHEGPV
WQVAWAHPMY GNILASCSYD RKVIIWKEEN GTWEKTHEHT GHDSSVNSVC WAPHDYGLIL
ACGSSDGAIS LLTYTGLGQW EVKKINNAHT IGCNAVSWAP AVVPGSLIDQ PSGQKPNYIK
KFASGGCDNL IKLWKEEEDG QWKEEQKLEA HSDWVRDVAW APSIGLPTST IASCSQDGRV
FVWTCDDASG NTWSPKLLHK FNDVVWHVSW SITANILAVS GGDNKVTLWK ESVDGQWVCI
SDVNKGQGPV STSVTEGQQN DQ
