SURF4_MOUSE
ID SURF4_MOUSE Reviewed; 269 AA.
AC Q64310;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Surfeit locus protein 4 {ECO:0000303|PubMed:2300057};
GN Name=Surf4 {ECO:0000303|PubMed:21976701, ECO:0000312|MGI:MGI:98445};
GN Synonyms=Surf-4 {ECO:0000303|PubMed:2300057};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ;
RX PubMed=2300057; DOI=10.1128/mcb.10.2.605-614.1990;
RA Huxley C., Fried M.;
RT "The mouse surfeit locus contains a cluster of six genes associated with
RT four CpG-rich islands in 32 kilobases of genomic DNA.";
RL Mol. Cell. Biol. 10:605-614(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=7540914; DOI=10.3109/09687689509027508;
RA Reeves J.E., Fried M.;
RT "The surf-4 gene encodes a novel 30 kDa integral membrane protein.";
RL Mol. Membr. Biol. 12:201-208(1995).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP INTERACTION WITH ZFYVE27 AND KIF5A.
RX PubMed=21976701; DOI=10.1091/mbc.e11-01-0068;
RA Matsuzaki F., Shirane M., Matsumoto M., Nakayama K.I.;
RT "Protrudin serves as an adaptor molecule that connects KIF5 and its cargoes
RT in vesicular transport during process formation.";
RL Mol. Biol. Cell 22:4602-4620(2011).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=31978056; DOI=10.1371/journal.pone.0227450;
RA Emmer B.T., Lascuna P.J., Tang V.T., Kotnik E.N., Saunders T.L.,
RA Khoriaty R., Ginsburg D.;
RT "Murine Surf4 is essential for early embryonic development.";
RL PLoS ONE 15:e0227450-e0227450(2020).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=33186557; DOI=10.1016/j.cmet.2020.10.020;
RA Wang X., Wang H., Xu B., Huang D., Nie C., Pu L., Zajac G.J.M., Yan H.,
RA Zhao J., Shi F., Emmer B.T., Lu J., Wang R., Dong X., Dai J., Zhou W.,
RA Wang C., Gao G., Wang Y., Willer C., Lu X., Zhu Y., Chen X.W.;
RT "Receptor-mediated ER export of lipoproteins controls lipid homeostasis in
RT mice and humans.";
RL Cell Metab. 33:350-366(2021).
CC -!- FUNCTION: Endoplasmic reticulum cargo receptor that mediates the export
CC of lipoproteins by recruiting cargos into COPII vesicles to facilitate
CC their secretion. Acts as a cargo receptor for lipoproteins bearing both
CC APOB and APOA1, thereby regulating lipoprotein delivery and the
CC maintenance of lipid homeostasis. Synergizes with the GTPase SAR1B to
CC mediate transport of circulating lipoproteins. Promotes the secretion
CC of PCSK9. Also mediates the efficient secretion of erythropoietin
CC (EPO). May also play a role in the maintenance of the architecture of
CC the endoplasmic reticulum-Golgi intermediate compartment and of the
CC Golgi. {ECO:0000250|UniProtKB:O15260}.
CC -!- SUBUNIT: Found in a complex composed at least of SURF4, TMED2 and
CC TMED10 (By similarity). May interact with LMAN1 (By similarity).
CC Interacts with ZFYVE27 and with KIF5A in a ZFYVE27-dependent manner
CC (PubMed:21976701). Interacts with STING1 (By similarity). Interacts
CC with SAR1B (By similarity). Interacts with TMEM41B (By similarity).
CC {ECO:0000250|UniProtKB:O15260, ECO:0000269|PubMed:21976701}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O15260}; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment
CC membrane {ECO:0000250|UniProtKB:O15260}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:O15260};
CC Multi-pass membrane protein {ECO:0000255}. Note=Cycles between the
CC endoplasmic reticulum and the Golgi. {ECO:0000250|UniProtKB:O15260}.
CC -!- DOMAIN: The di-lysine motif confers endoplasmic reticulum localization
CC for type I membrane proteins. {ECO:0000250|UniProtKB:O15260}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality between 3.5 and 9.5 dpc
CC (PubMed:31978056). Conditional deletion in the liver depletes plasma
CC lipids and protects mice from atherosclerosis (PubMed:33186557).
CC {ECO:0000269|PubMed:31978056, ECO:0000269|PubMed:33186557}.
CC -!- SIMILARITY: Belongs to the SURF4 family. {ECO:0000305}.
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DR EMBL; M62606; AAA40155.1; -; Genomic_DNA.
DR EMBL; M62601; AAA40155.1; JOINED; Genomic_DNA.
DR EMBL; M62602; AAA40155.1; JOINED; Genomic_DNA.
DR EMBL; M62603; AAA40155.1; JOINED; Genomic_DNA.
DR EMBL; M62605; AAA40155.1; JOINED; Genomic_DNA.
DR EMBL; M63114; AAA40156.1; -; mRNA.
DR EMBL; BC003280; AAH03280.1; -; mRNA.
DR EMBL; BC027352; AAH27352.1; -; mRNA.
DR CCDS; CCDS15817.1; -.
DR PIR; A34727; A34727.
DR RefSeq; NP_035642.1; NM_011512.3.
DR AlphaFoldDB; Q64310; -.
DR BioGRID; 203581; 9.
DR IntAct; Q64310; 1.
DR STRING; 10090.ENSMUSP00000015011; -.
DR iPTMnet; Q64310; -.
DR PhosphoSitePlus; Q64310; -.
DR SwissPalm; Q64310; -.
DR EPD; Q64310; -.
DR jPOST; Q64310; -.
DR MaxQB; Q64310; -.
DR PaxDb; Q64310; -.
DR PRIDE; Q64310; -.
DR ProteomicsDB; 258780; -.
DR Antibodypedia; 31854; 137 antibodies from 19 providers.
DR DNASU; 20932; -.
DR Ensembl; ENSMUST00000015011; ENSMUSP00000015011; ENSMUSG00000014867.
DR GeneID; 20932; -.
DR KEGG; mmu:20932; -.
DR UCSC; uc008iwl.2; mouse.
DR CTD; 6836; -.
DR MGI; MGI:98445; Surf4.
DR VEuPathDB; HostDB:ENSMUSG00000014867; -.
DR eggNOG; KOG3998; Eukaryota.
DR GeneTree; ENSGT00530000064123; -.
DR HOGENOM; CLU_056195_0_0_1; -.
DR InParanoid; Q64310; -.
DR OMA; RHRHFPW; -.
DR OrthoDB; 1272733at2759; -.
DR PhylomeDB; Q64310; -.
DR TreeFam; TF300001; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR BioGRID-ORCS; 20932; 7 hits in 71 CRISPR screens.
DR ChiTaRS; Surf4; mouse.
DR PRO; PR:Q64310; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q64310; protein.
DR Bgee; ENSMUSG00000014867; Expressed in seminal vesicle and 264 other tissues.
DR ExpressionAtlas; Q64310; baseline and differential.
DR Genevisible; Q64310; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISO:MGI.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0038024; F:cargo receptor activity; ISS:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; ISO:MGI.
DR GO; GO:0055088; P:lipid homeostasis; ISS:UniProtKB.
DR GO; GO:0042953; P:lipoprotein transport; ISS:UniProtKB.
DR GO; GO:0010638; P:positive regulation of organelle organization; ISO:MGI.
DR GO; GO:0032368; P:regulation of lipid transport; ISS: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 1: Evidence at protein level;
KW Endoplasmic reticulum; Golgi apparatus; Membrane; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..269
FT /note="Surfeit locus protein 4"
FT /id="PRO_0000127665"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 266..269
FT /note="Di-lysine motif"
FT /evidence="ECO:0000250|UniProtKB:O15260"
SQ SEQUENCE 269 AA; 30381 MW; CC1F5219400E52F8 CRC64;
MGQNDLMGTA EDFADQFLRV TKQYLPHVAR LCLISTFLED GIRMWFQWSE QRDYIDTTWS
CGYLLASSFV FLNLLGQLTG CVLVLSRNFV QYACFGLFGI IALQTIAYSI LWDLKFLMRN
LALGGGLLLL LAESRSEGKS MFAGVPTMRE SSPKQYMQLG GRVLLVLMFM TLLHFDASFF
SIIQNIVGTA LMILVAIGFK TKLAALTLVV WLFAINVYFN AFWTIPVYKP MHDFLKYDFF
QTMSVIGGLL LVVALGPGGV SMDEKKKEW
