SURF4_HUMAN
ID SURF4_HUMAN Reviewed; 269 AA.
AC O15260; B7Z6A4; O60923; Q5T8U6; Q9UNZ0; Q9UNZ1;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 3.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Surfeit locus protein 4 {ECO:0000303|PubMed:9740673};
GN Name=SURF4 {ECO:0000303|PubMed:18287528, ECO:0000312|HGNC:HGNC:11476};
GN Synonyms=SURF-4 {ECO:0000303|PubMed:9740673};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Pituitary;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-261.
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 258-269.
RX PubMed=9740673; DOI=10.1006/geno.1998.5372;
RA Duhig T., Ruhrberg C., Mor O., Fried M.;
RT "The human Surfeit locus.";
RL Genomics 52:72-78(1998).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=15308636; DOI=10.1074/jbc.m406644200;
RA Breuza L., Halbeisen R., Jenoe P., Otte S., Barlowe C., Hong W.,
RA Hauri H.-P.;
RT "Proteomics of endoplasmic reticulum-Golgi intermediate compartment (ERGIC)
RT membranes from brefeldin A-treated HepG2 cells identifies ERGIC-32, a new
RT cycling protein that interacts with human Erv46.";
RL J. Biol. Chem. 279:47242-47253(2004).
RN [9]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH TMED2 AND TMED10, INTERACTION
RP WITH LMAN1, SUBCELLULAR LOCATION, MUTAGENESIS OF 265-LYS--LYS-267, AND
RP DI-LYSINE MOTIF.
RX PubMed=18287528; DOI=10.1091/mbc.e07-10-0989;
RA Mitrovic S., Ben-Tekaya H., Koegler E., Gruenberg J., Hauri H.-P.;
RT "The cargo receptors Surf4, endoplasmic reticulum-Golgi intermediate
RT compartment (ERGIC)-53, and p25 are required to maintain the architecture
RT of ERGIC and Golgi.";
RL Mol. Biol. Cell 19:1976-1990(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=30251625; DOI=10.7554/elife.38839;
RA Emmer B.T., Hesketh G.G., Kotnik E., Tang V.T., Lascuna P.J., Xiang J.,
RA Gingras A.C., Chen X.W., Ginsburg D.;
RT "The cargo receptor SURF4 promotes the efficient cellular secretion of
RT PCSK9.";
RL Elife 7:0-0(2018).
RN [14]
RP FUNCTION.
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).
RN [15]
RP INTERACTION WITH STING1.
RX PubMed=29251827; DOI=10.1002/pmic.201700403;
RA Shang J., Xia T., Han Q.Q., Zhao X., Hu M.M., Shu H.B., Guo L.;
RT "Quantitative Proteomics Identified TTC4 as a TBK1 Interactor and a
RT Positive Regulator of SeV-Induced Innate Immunity.";
RL Proteomics 18:0-0(2018).
RN [16]
RP FUNCTION.
RX PubMed=32989016; DOI=10.1128/mcb.00180-20;
RA Lin Z., King R., Tang V., Myers G., Balbin-Cuesta G., Friedman A.,
RA McGee B., Desch K., Ozel A.B., Siemieniak D., Reddy P., Emmer B.,
RA Khoriaty R.;
RT "The endoplasmic reticulum cargo receptor SURF4 facilitates efficient
RT erythropoietin secretion.";
RL Mol. Cell. Biol. 40:0-0(2020).
RN [17]
RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 265-LYS--LYS-267, DI-LYSINE
RP MOTIF, AND INTERACTION WITH SAR1B.
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).
RN [18]
RP INTERACTION WITH TMEM41B.
RX PubMed=34015269; DOI=10.1016/j.cmet.2021.05.006;
RA Huang D., Xu B., Liu L., Wu L., Zhu Y., Ghanbarpour A., Wang Y., Chen F.J.,
RA Lyu J., Hu Y., Kang Y., Zhou W., Wang X., Ding W., Li X., Jiang Z.,
RA Chen J., Zhang X., Zhou H., Li J.Z., Guo C., Zheng W., Zhang X., Li P.,
RA Melia T., Reinisch K., Chen X.W.;
RT "TMEM41B acts as an ER scramblase required for lipoprotein biogenesis and
RT lipid homeostasis.";
RL Cell Metab. 0:0-0(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 (PubMed:30251625, PubMed:29643117, PubMed:33186557).
CC Acts as a cargo receptor for lipoproteins bearing both APOB and APOA1,
CC thereby regulating lipoprotein delivery and the maintenance of lipid
CC homeostasis (PubMed:29643117, PubMed:33186557). Synergizes with the
CC GTPase SAR1B to mediate transport of circulating lipoproteins
CC (PubMed:33186557). Promotes the secretion of PCSK9 (PubMed:30251625).
CC Also mediates the efficient secretion of erythropoietin (EPO)
CC (PubMed:32989016). May also play a role in the maintenance of the
CC architecture of the endoplasmic reticulum-Golgi intermediate
CC compartment and of the Golgi (PubMed:18287528).
CC {ECO:0000269|PubMed:18287528, ECO:0000269|PubMed:29643117,
CC ECO:0000269|PubMed:30251625, ECO:0000269|PubMed:32989016,
CC ECO:0000269|PubMed:33186557}.
CC -!- SUBUNIT: Found in a complex composed at least of SURF4, TMED2 and
CC TMED10 (PubMed:18287528). May interact with LMAN1 (PubMed:18287528).
CC Interacts with ZFYVE27 and with KIF5A in a ZFYVE27-dependent manner (By
CC similarity). Interacts with STING1 (PubMed:29251827). Interacts with
CC SAR1B (PubMed:33186557). Interacts with TMEM41B (PubMed:34015269).
CC {ECO:0000250|UniProtKB:Q64310, ECO:0000269|PubMed:18287528,
CC ECO:0000269|PubMed:29251827, ECO:0000269|PubMed:33186557,
CC ECO:0000269|PubMed:34015269}.
CC -!- INTERACTION:
CC O15260; P49257: LMAN1; NbExp=3; IntAct=EBI-1044848, EBI-1057738;
CC O15260; Q86WV6: STING1; NbExp=3; IntAct=EBI-1044848, EBI-2800345;
CC O15260; Q8VCW4: Unc93b1; Xeno; NbExp=2; IntAct=EBI-1044848, EBI-6116986;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15308636, ECO:0000269|PubMed:18287528,
CC ECO:0000269|PubMed:30251625, ECO:0000269|PubMed:33186557}; Multi-pass
CC membrane protein {ECO:0000255}. Endoplasmic reticulum-Golgi
CC intermediate compartment membrane {ECO:0000269|PubMed:18287528}; Multi-
CC pass membrane protein {ECO:0000255}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:18287528, ECO:0000269|PubMed:30251625,
CC ECO:0000269|PubMed:33186557}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Cycles between the endoplasmic reticulum and the
CC Golgi. {ECO:0000269|PubMed:18287528, ECO:0000269|PubMed:33186557}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O15260-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15260-2; Sequence=VSP_006307, VSP_006308;
CC Name=3;
CC IsoId=O15260-3; Sequence=VSP_054686, VSP_054687;
CC -!- DOMAIN: The di-lysine motif confers endoplasmic reticulum localization
CC for type I membrane proteins. {ECO:0000269|PubMed:18287528}.
CC -!- SIMILARITY: Belongs to the SURF4 family. {ECO:0000305}.
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DR EMBL; AF078866; AAD44498.1; -; mRNA.
DR EMBL; AF078867; AAD44499.1; -; mRNA.
DR EMBL; AK300004; BAH13190.1; -; mRNA.
DR EMBL; AK315488; BAG37872.1; -; mRNA.
DR EMBL; AL158826; CAI12840.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW88071.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW88074.1; -; Genomic_DNA.
DR EMBL; BC018741; AAH18741.1; -; mRNA.
DR EMBL; BC111023; AAI11024.1; -; mRNA.
DR EMBL; Y14820; CAA75099.1; -; mRNA.
DR EMBL; Y17214; CAA76692.1; -; Genomic_DNA.
DR CCDS; CCDS65177.1; -. [O15260-3]
DR CCDS; CCDS65178.1; -. [O15260-2]
DR CCDS; CCDS6968.1; -. [O15260-1]
DR RefSeq; NP_001267718.1; NM_001280789.1. [O15260-2]
DR RefSeq; NP_001267721.1; NM_001280792.1. [O15260-3]
DR RefSeq; NP_149351.1; NM_033161.3. [O15260-1]
DR AlphaFoldDB; O15260; -.
DR BioGRID; 112703; 225.
DR CORUM; O15260; -.
DR IntAct; O15260; 76.
DR MINT; O15260; -.
DR STRING; 9606.ENSP00000361057; -.
DR TCDB; 9.B.214.1.2; the er to golgi transport factor (er/g-tf) family.
DR CarbonylDB; O15260; -.
DR GlyGen; O15260; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O15260; -.
DR MetOSite; O15260; -.
DR PhosphoSitePlus; O15260; -.
DR SwissPalm; O15260; -.
DR BioMuta; SURF4; -.
DR EPD; O15260; -.
DR jPOST; O15260; -.
DR MassIVE; O15260; -.
DR MaxQB; O15260; -.
DR PaxDb; O15260; -.
DR PeptideAtlas; O15260; -.
DR PRIDE; O15260; -.
DR ProteomicsDB; 48549; -. [O15260-1]
DR ProteomicsDB; 48550; -. [O15260-2]
DR ProteomicsDB; 6763; -.
DR TopDownProteomics; O15260-1; -. [O15260-1]
DR Antibodypedia; 31854; 137 antibodies from 19 providers.
DR DNASU; 6836; -.
DR Ensembl; ENST00000371989.8; ENSP00000361057.3; ENSG00000148248.14. [O15260-1]
DR Ensembl; ENST00000485435.6; ENSP00000419853.2; ENSG00000148248.14. [O15260-2]
DR Ensembl; ENST00000545297.5; ENSP00000446061.1; ENSG00000148248.14. [O15260-3]
DR Ensembl; ENST00000626303.2; ENSP00000487537.1; ENSG00000280951.3. [O15260-2]
DR Ensembl; ENST00000629119.2; ENSP00000486869.1; ENSG00000280951.3. [O15260-3]
DR Ensembl; ENST00000629578.3; ENSP00000486049.1; ENSG00000280951.3. [O15260-1]
DR GeneID; 6836; -.
DR KEGG; hsa:6836; -.
DR MANE-Select; ENST00000371989.8; ENSP00000361057.3; NM_033161.4; NP_149351.1.
DR UCSC; uc004cdj.5; human. [O15260-1]
DR CTD; 6836; -.
DR DisGeNET; 6836; -.
DR GeneCards; SURF4; -.
DR HGNC; HGNC:11476; SURF4.
DR HPA; ENSG00000148248; Low tissue specificity.
DR MIM; 185660; gene.
DR neXtProt; NX_O15260; -.
DR OpenTargets; ENSG00000148248; -.
DR PharmGKB; PA36261; -.
DR VEuPathDB; HostDB:ENSG00000148248; -.
DR eggNOG; KOG3998; Eukaryota.
DR GeneTree; ENSGT00530000064123; -.
DR HOGENOM; CLU_056195_0_0_1; -.
DR InParanoid; O15260; -.
DR OMA; RHRHFPW; -.
DR OrthoDB; 1443136at2759; -.
DR PhylomeDB; O15260; -.
DR TreeFam; TF300001; -.
DR PathwayCommons; O15260; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR SignaLink; O15260; -.
DR BioGRID-ORCS; 6836; 46 hits in 1081 CRISPR screens.
DR ChiTaRS; SURF4; human.
DR GeneWiki; SURF4; -.
DR GenomeRNAi; 6836; -.
DR Pharos; O15260; Tbio.
DR PRO; PR:O15260; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; O15260; protein.
DR Bgee; ENSG00000148248; Expressed in islet of Langerhans and 95 other tissues.
DR ExpressionAtlas; O15260; baseline and differential.
DR Genevisible; O15260; HS.
DR GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0030133; C:transport vesicle; TAS:Reactome.
DR GO; GO:0038024; F:cargo receptor activity; IDA:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR GO; GO:0055088; P:lipid homeostasis; IDA:UniProtKB.
DR GO; GO:0042953; P:lipoprotein transport; IDA:UniProtKB.
DR GO; GO:0010638; P:positive regulation of organelle organization; IMP:UniProtKB.
DR GO; GO:0032368; P:regulation of lipid transport; 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 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Golgi apparatus; Membrane;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:25944712"
FT CHAIN 2..269
FT /note="Surfeit locus protein 4"
FT /id="PRO_0000127664"
FT TRANSMEM 64..84
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 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 266..269
FT /note="Di-lysine motif"
FT /evidence="ECO:0000269|PubMed:18287528"
FT VAR_SEQ 120..128
FT /note="NLALGGGLL -> LSRTSWAQL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054686"
FT VAR_SEQ 129..269
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054687"
FT VAR_SEQ 157..159
FT /note="MQL -> LPG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10931946"
FT /id="VSP_006307"
FT VAR_SEQ 160..269
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10931946"
FT /id="VSP_006308"
FT MUTAGEN 265..267
FT /note="KKK->SSS,AAA: Targeted to the Golgi."
FT /evidence="ECO:0000269|PubMed:18287528,
FT ECO:0000269|PubMed:33186557"
FT CONFLICT 130
FT /note="L -> V (in Ref. 6; CAA75099)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 269 AA; 30394 MW; 03366E29882B97A5 CRC64;
MGQNDLMGTA EDFADQFLRV TKQYLPHVAR LCLISTFLED GIRMWFQWSE QRDYIDTTWN
CGYLLASSFV FLNLLGQLTG CVLVLSRNFV QYACFGLFGI IALQTIAYSI LWDLKFLMRN
LALGGGLLLL LAESRSEGKS MFAGVPTMRE SSPKQYMQLG GRVLLVLMFM TLLHFDASFF
SIVQNIVGTA LMILVAIGFK TKLAALTLVV WLFAINVYFN AFWTIPVYKP MHDFLKYDFF
QTMSVIGGLL LVVALGPGGV SMDEKKKEW
