SURF4_CAEEL
ID SURF4_CAEEL Reviewed; 277 AA.
AC Q18864; O18006;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Surfeit locus protein 4 homolog {ECO:0000305};
GN Name=sft-4 {ECO:0000303|PubMed:29643117};
GN Synonyms=surf-4 {ECO:0000303|PubMed:8816471}; ORFNames=C54H2.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8816471; DOI=10.1128/mcb.16.10.5591;
RA Armes N., Fried M.;
RT "Surfeit locus gene homologs are widely distributed in invertebrate
RT genomes.";
RL Mol. Cell. Biol. 16:5591-5596(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=29643117; DOI=10.1083/jcb.201708115;
RA Saegusa K., Sato M., Morooka N., Hara T., Sato K.;
RT "SFT-4/Surf4 control ER export of soluble cargo proteins and participate in
RT ER exit site organization.";
RL J. Cell Biol. 217:2073-2085(2018).
CC -!- FUNCTION: Endoplasmic reticulum cargo receptor that mediates the export
CC of the yolk proteins from intestinal cells by recruiting cargos into
CC COPII vesicles to facilitate their secretion (PubMed:29643117).
CC Required for the endoplasmic reticulum export of the yolk protein vit-
CC 2, which is synthesized as a lipoprotein complex, from intestinal cells
CC (PubMed:29643117). Involved in endoplasmic reticulum exit sites (ERES)
CC organization (PubMed:29643117). {ECO:0000269|PubMed:29643117}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:29643117}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Predominantly localizes at endoplasmic reticulum
CC exit sites (ERES). {ECO:0000269|PubMed:29643117}.
CC -!- DOMAIN: The di-lysine motif confers endoplasmic reticulum localization
CC for type I membrane proteins. {ECO:0000250|UniProtKB:O15260}.
CC -!- DISRUPTION PHENOTYPE: High rate of embryonic and larval lethality
CC (PubMed:29643117). Some mutants reach adulthood but display severe
CC accumulation of vit-2 in large granule-like structures in intestinal
CC cells (PubMed:29643117). {ECO:0000269|PubMed:29643117}.
CC -!- SIMILARITY: Belongs to the SURF4 family. {ECO:0000305}.
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DR EMBL; Y14949; CAA75173.1; -; mRNA.
DR EMBL; FO080839; CCD67143.1; -; Genomic_DNA.
DR PIR; T29611; T29611.
DR RefSeq; NP_508970.1; NM_076569.8.
DR AlphaFoldDB; Q18864; -.
DR BioGRID; 45776; 5.
DR STRING; 6239.C54H2.5.1; -.
DR EPD; Q18864; -.
DR PaxDb; Q18864; -.
DR PeptideAtlas; Q18864; -.
DR EnsemblMetazoa; C54H2.5.1; C54H2.5.1; WBGene00004788.
DR GeneID; 180843; -.
DR KEGG; cel:CELE_C54H2.5; -.
DR UCSC; C54H2.5.1; c. elegans.
DR CTD; 180843; -.
DR WormBase; C54H2.5; CE06987; WBGene00004788; sft-4.
DR eggNOG; KOG3998; Eukaryota.
DR GeneTree; ENSGT00530000064123; -.
DR HOGENOM; CLU_056195_0_0_1; -.
DR InParanoid; Q18864; -.
DR OMA; RHRHFPW; -.
DR OrthoDB; 1272733at2759; -.
DR PhylomeDB; Q18864; -.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR PRO; PR:Q18864; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00004788; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISS:WormBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:WormBase.
DR GO; GO:0038024; F:cargo receptor activity; IDA:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IGI:WormBase.
DR GO; GO:0040027; P:negative regulation of vulval development; IGI:WormBase.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:WormBase.
DR GO; GO:0032527; P:protein exit from endoplasmic reticulum; IDA:UniProtKB.
DR InterPro; IPR045214; Surf1/Surf4.
DR InterPro; IPR002995; Surf4.
DR PANTHER; PTHR23427; PTHR23427; 1.
DR Pfam; PF02077; SURF4; 1.
DR PROSITE; PS01339; SURF4; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Membrane; Protein transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..277
FT /note="Surfeit locus protein 4 homolog"
FT /id="PRO_0000127668"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 274..277
FT /note="Di-lysine motif"
FT /evidence="ECO:0000255"
FT CONFLICT 17
FT /note="A -> R (in Ref. 1; CAA75173)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 277 AA; 31813 MW; 8FF2848676CC0245 CRC64;
MNQFRAPGGQ NEMLAKAEDA AEDFFRKTRT YLPHIARLCL VSTFLEDGIR MYFQWDDQKQ
FMQESWSCGW FIATLFVIYN FFGQFIPVLM IMLRKKVLVA CGILASIVIL QTIAYHILWD
LKFLARNIAV GGGLLLLLAE TQEEKASLFA GVPTMGDSNK PKSYMLLAGR VLLIFMFMSL
MHFEMSFMQV LEIVVGFALI TLVSIGYKTK LSAIVLVIWL FGLNLWLNAW WTIPSDRFYR
DFMKYDFFQT MSVIGGLLLV IAYGPGGVSV DDYKKRW
