Full text data of SURF4
SURF4
(SURF-4)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Surfeit locus protein 4
Surfeit locus protein 4
UniProt
O15260
ID SURF4_HUMAN Reviewed; 269 AA.
AC O15260; O60923; Q5T8U6; Q9UNZ0; Q9UNZ1;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2000, sequence version 3.
DT 22-JAN-2014, entry version 119.
DE RecName: Full=Surfeit locus protein 4;
GN Name=SURF4; Synonyms=SURF-4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis 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] (ISOFORM 1).
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA 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.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA 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.,
RA Rogers J., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-261.
RX PubMed=7540914;
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
RT (ERGIC) membranes from brefeldin A-treated HepG2 cells identifies
RT ERGIC-32, a new 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,
RP INTERACTION WITH LMAN1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 265-LYS--LYS-267.
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
RT architecture 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.,
RA Buerckstuemmer T., 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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: May play a role in the maintenance of the architecture
CC of the endoplasmic reticulum-Golgi intermediate compartment and of
CC the Golgi.
CC -!- SUBUNIT: Found in a complex composed at least of SURF4, TMED2 and
CC TMED10. May interact with LMAN1.
CC -!- INTERACTION:
CC P49257:LMAN1; NbExp=3; IntAct=EBI-1044848, EBI-1057738;
CC Q86WV6:TMEM173; NbExp=2; IntAct=EBI-1044848, EBI-2800345;
CC Q8VCW4:Unc93b1 (xeno); NbExp=2; IntAct=EBI-1044848, EBI-6116986;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein. Endoplasmic reticulum-Golgi intermediate
CC compartment membrane; Multi-pass membrane protein. Golgi apparatus
CC membrane; Multi-pass membrane protein. Note=Cycles between the
CC endoplasmic reticulum and the Golgi.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O15260-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15260-2; Sequence=VSP_006307, VSP_006308;
CC -!- DOMAIN: The di-lysine motif confers endoplasmic reticulum
CC localization for type I membrane proteins.
CC -!- SIMILARITY: Belongs to the SURF4 family.
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DR EMBL; AF078866; AAD44498.1; -; mRNA.
DR EMBL; AF078867; AAD44499.1; -; mRNA.
DR EMBL; AK315488; BAG37872.1; -; mRNA.
DR EMBL; AL158826; CAI12840.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW88071.1; -; 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 RefSeq; NP_001267718.1; NM_001280789.1.
DR RefSeq; NP_149351.1; NM_033161.3.
DR UniGene; Hs.512465; -.
DR ProteinModelPortal; O15260; -.
DR IntAct; O15260; 8.
DR MINT; MINT-2998714; -.
DR STRING; 9606.ENSP00000361057; -.
DR PhosphoSite; O15260; -.
DR PaxDb; O15260; -.
DR PRIDE; O15260; -.
DR DNASU; 6836; -.
DR Ensembl; ENST00000371989; ENSP00000361057; ENSG00000148248.
DR Ensembl; ENST00000485435; ENSP00000419853; ENSG00000148248.
DR Ensembl; ENST00000561745; ENSP00000457043; ENSG00000260181.
DR GeneID; 6836; -.
DR KEGG; hsa:6836; -.
DR UCSC; uc004cdj.3; human.
DR CTD; 6836; -.
DR GeneCards; GC09M136228; -.
DR HGNC; HGNC:11476; SURF4.
DR MIM; 185660; gene.
DR neXtProt; NX_O15260; -.
DR PharmGKB; PA36261; -.
DR eggNOG; COG2259; -.
DR HOGENOM; HOG000206959; -.
DR HOVERGEN; HBG054238; -.
DR InParanoid; O15260; -.
DR OMA; DQLWYLQ; -.
DR PhylomeDB; O15260; -.
DR ChiTaRS; Surf4; human.
DR GeneWiki; SURF4; -.
DR GenomeRNAi; 6836; -.
DR NextBio; 26687; -.
DR PRO; PR:O15260; -.
DR ArrayExpress; O15260; -.
DR Bgee; O15260; -.
DR CleanEx; HS_SURF4; -.
DR Genevestigator; O15260; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR GO; GO:0010638; P:positive regulation of organelle organization; IMP:UniProtKB.
DR InterPro; IPR002995; Surf4.
DR Pfam; PF02077; SURF4; 1.
DR PROSITE; PS01339; SURF4; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Endoplasmic reticulum;
KW Golgi apparatus; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1 269 Surfeit locus protein 4.
FT /FTId=PRO_0000127664.
FT TRANSMEM 64 84 Helical; (Potential).
FT TRANSMEM 92 112 Helical; (Potential).
FT TRANSMEM 179 199 Helical; (Potential).
FT TRANSMEM 203 223 Helical; (Potential).
FT TRANSMEM 239 259 Helical; (Potential).
FT MOTIF 266 269 Di-lysine motif.
FT VAR_SEQ 157 159 MQL -> LPG (in isoform 2).
FT /FTId=VSP_006307.
FT VAR_SEQ 160 269 Missing (in isoform 2).
FT /FTId=VSP_006308.
FT MUTAGEN 265 267 KKK->SSS: Targeted to the Golgi.
FT CONFLICT 130 130 L -> V (in Ref. 6; CAA75099).
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
//
ID SURF4_HUMAN Reviewed; 269 AA.
AC O15260; O60923; Q5T8U6; Q9UNZ0; Q9UNZ1;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2000, sequence version 3.
DT 22-JAN-2014, entry version 119.
DE RecName: Full=Surfeit locus protein 4;
GN Name=SURF4; Synonyms=SURF-4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis 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] (ISOFORM 1).
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA 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.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA 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.,
RA Rogers J., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-261.
RX PubMed=7540914;
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
RT (ERGIC) membranes from brefeldin A-treated HepG2 cells identifies
RT ERGIC-32, a new 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,
RP INTERACTION WITH LMAN1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 265-LYS--LYS-267.
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
RT architecture 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.,
RA Buerckstuemmer T., 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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: May play a role in the maintenance of the architecture
CC of the endoplasmic reticulum-Golgi intermediate compartment and of
CC the Golgi.
CC -!- SUBUNIT: Found in a complex composed at least of SURF4, TMED2 and
CC TMED10. May interact with LMAN1.
CC -!- INTERACTION:
CC P49257:LMAN1; NbExp=3; IntAct=EBI-1044848, EBI-1057738;
CC Q86WV6:TMEM173; NbExp=2; IntAct=EBI-1044848, EBI-2800345;
CC Q8VCW4:Unc93b1 (xeno); NbExp=2; IntAct=EBI-1044848, EBI-6116986;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein. Endoplasmic reticulum-Golgi intermediate
CC compartment membrane; Multi-pass membrane protein. Golgi apparatus
CC membrane; Multi-pass membrane protein. Note=Cycles between the
CC endoplasmic reticulum and the Golgi.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O15260-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15260-2; Sequence=VSP_006307, VSP_006308;
CC -!- DOMAIN: The di-lysine motif confers endoplasmic reticulum
CC localization for type I membrane proteins.
CC -!- SIMILARITY: Belongs to the SURF4 family.
CC -----------------------------------------------------------------------
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CC Distributed under the Creative Commons Attribution-NoDerivs License
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DR EMBL; AF078866; AAD44498.1; -; mRNA.
DR EMBL; AF078867; AAD44499.1; -; mRNA.
DR EMBL; AK315488; BAG37872.1; -; mRNA.
DR EMBL; AL158826; CAI12840.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW88071.1; -; 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 RefSeq; NP_001267718.1; NM_001280789.1.
DR RefSeq; NP_149351.1; NM_033161.3.
DR UniGene; Hs.512465; -.
DR ProteinModelPortal; O15260; -.
DR IntAct; O15260; 8.
DR MINT; MINT-2998714; -.
DR STRING; 9606.ENSP00000361057; -.
DR PhosphoSite; O15260; -.
DR PaxDb; O15260; -.
DR PRIDE; O15260; -.
DR DNASU; 6836; -.
DR Ensembl; ENST00000371989; ENSP00000361057; ENSG00000148248.
DR Ensembl; ENST00000485435; ENSP00000419853; ENSG00000148248.
DR Ensembl; ENST00000561745; ENSP00000457043; ENSG00000260181.
DR GeneID; 6836; -.
DR KEGG; hsa:6836; -.
DR UCSC; uc004cdj.3; human.
DR CTD; 6836; -.
DR GeneCards; GC09M136228; -.
DR HGNC; HGNC:11476; SURF4.
DR MIM; 185660; gene.
DR neXtProt; NX_O15260; -.
DR PharmGKB; PA36261; -.
DR eggNOG; COG2259; -.
DR HOGENOM; HOG000206959; -.
DR HOVERGEN; HBG054238; -.
DR InParanoid; O15260; -.
DR OMA; DQLWYLQ; -.
DR PhylomeDB; O15260; -.
DR ChiTaRS; Surf4; human.
DR GeneWiki; SURF4; -.
DR GenomeRNAi; 6836; -.
DR NextBio; 26687; -.
DR PRO; PR:O15260; -.
DR ArrayExpress; O15260; -.
DR Bgee; O15260; -.
DR CleanEx; HS_SURF4; -.
DR Genevestigator; O15260; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR GO; GO:0010638; P:positive regulation of organelle organization; IMP:UniProtKB.
DR InterPro; IPR002995; Surf4.
DR Pfam; PF02077; SURF4; 1.
DR PROSITE; PS01339; SURF4; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Endoplasmic reticulum;
KW Golgi apparatus; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1 269 Surfeit locus protein 4.
FT /FTId=PRO_0000127664.
FT TRANSMEM 64 84 Helical; (Potential).
FT TRANSMEM 92 112 Helical; (Potential).
FT TRANSMEM 179 199 Helical; (Potential).
FT TRANSMEM 203 223 Helical; (Potential).
FT TRANSMEM 239 259 Helical; (Potential).
FT MOTIF 266 269 Di-lysine motif.
FT VAR_SEQ 157 159 MQL -> LPG (in isoform 2).
FT /FTId=VSP_006307.
FT VAR_SEQ 160 269 Missing (in isoform 2).
FT /FTId=VSP_006308.
FT MUTAGEN 265 267 KKK->SSS: Targeted to the Golgi.
FT CONFLICT 130 130 L -> V (in Ref. 6; CAA75099).
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
//
MIM
185660
*RECORD*
*FIELD* NO
185660
*FIELD* TI
*185660 SURFEIT 4; SURF4
;;ERV29, S. CEREVISIAE, HOMOLOG OF; ERV29
*FIELD* TX
For background information on the surfeit genes, see SURF1 (185620).
read more
CLONING
Using PCR with primers based on the sequence of mouse Surf4 to screen a
HeLa cell cDNA library, Reeves and Fried (1995) obtained a cDNA encoding
human SURF4. The deduced 269-amino acid protein, which is 60% and 99%
identical to the worm and mouse proteins, respectively, contains 7
transmembrane segments, a predicted luminal N terminus, multiple
phosphorylation sites, and a double-lysine retrieval motif at the C
terminus. Immunoblot analysis showed expression of a 30-kD membrane
protein. Immunofluorescence microscopy demonstrated cytoplasmic
expression.
Using Northern blot analysis, Garson et al. (1996) detected 3 variants
of mouse Surf4 that were ubiquitously expressed, although the levels of
each transcript varied between tissues.
GENE FUNCTION
Belden and Barlowe (2001) showed that Erv29, the yeast homolog of SURF4,
is directly required for packaging glycosylated pro-alpha-factor (Gpaf)
into COPII (see COPA; 601924) vesicles. Subcellular fractionation
experiments indicated that Erv29 is equally distributed between
endoplasmic reticulum (ER) and Golgi membranes. Increased expression of
Erv29 in the ER alleviated the accumulation of Gpaf. Belden and Barlowe
(2001) proposed that Erv29 binds to fully folded Gpaf and probably to
other soluble secretory cargo in the ER, after which the Erv29-cargo
complexes are packaged into COPII vesicles for transport to the Golgi
complex. The authors noted that similar mechanisms have been postulated
for ERGIC1 (LMAN1; 601567).
GENE STRUCTURE
Duhig et al. (1998) stated that the 5-prime end of each of the surfeit
genes, including SURF4, is contained within a CpG island. Although the
mouse Surf2 (185630) and Surf4 genes overlap at their 3-prime ends,
human SURF2 and SURF4 are separated by 302 bp due to a much shorter
3-prime UTR in the human SURF2 gene.
MAPPING
By contig analysis, Duhig et al. (1998) mapped the SURF4 gene to the
telomeric end of the surfeit locus on chromosome 9q34.
*FIELD* RF
1. Belden, W. J.; Barlowe, C.: Role of Erv29p in collecting soluble
secretory proteins into ER-derived transport vesicles. Science 294:
1528-1531, 2001.
2. Duhig, T.; Ruhrberg, C.; Mor, O.; Fried, M.: The human surfeit
locus. Genomics 52: 72-78, 1998.
3. Garson, K.; Duhig, T.; Fried, M.: Tissue-specific processing of
the Surf-5 and Surf-4 mRNAs. Gene Expr. 6: 209-218, 1996.
4. Reeves, J. E.; Fried, M.: The surf-4 gene encodes a novel 30 kDa
integral membrane protein. Molec. Membr. Biol. 12: 201-208, 1995.
*FIELD* CN
Patricia A. Hartz - updated: 11/10/2008
Paul J. Converse - updated: 11/28/2001
*FIELD* CD
Victor A. McKusick: 8/29/1989
*FIELD* ED
mgross: 12/05/2008
terry: 11/10/2008
terry: 7/26/2006
mgross: 11/28/2001
dkim: 7/16/1998
supermim: 3/16/1992
supermim: 3/20/1990
supermim: 2/20/1990
ddp: 10/27/1989
root: 8/29/1989
*RECORD*
*FIELD* NO
185660
*FIELD* TI
*185660 SURFEIT 4; SURF4
;;ERV29, S. CEREVISIAE, HOMOLOG OF; ERV29
*FIELD* TX
For background information on the surfeit genes, see SURF1 (185620).
read more
CLONING
Using PCR with primers based on the sequence of mouse Surf4 to screen a
HeLa cell cDNA library, Reeves and Fried (1995) obtained a cDNA encoding
human SURF4. The deduced 269-amino acid protein, which is 60% and 99%
identical to the worm and mouse proteins, respectively, contains 7
transmembrane segments, a predicted luminal N terminus, multiple
phosphorylation sites, and a double-lysine retrieval motif at the C
terminus. Immunoblot analysis showed expression of a 30-kD membrane
protein. Immunofluorescence microscopy demonstrated cytoplasmic
expression.
Using Northern blot analysis, Garson et al. (1996) detected 3 variants
of mouse Surf4 that were ubiquitously expressed, although the levels of
each transcript varied between tissues.
GENE FUNCTION
Belden and Barlowe (2001) showed that Erv29, the yeast homolog of SURF4,
is directly required for packaging glycosylated pro-alpha-factor (Gpaf)
into COPII (see COPA; 601924) vesicles. Subcellular fractionation
experiments indicated that Erv29 is equally distributed between
endoplasmic reticulum (ER) and Golgi membranes. Increased expression of
Erv29 in the ER alleviated the accumulation of Gpaf. Belden and Barlowe
(2001) proposed that Erv29 binds to fully folded Gpaf and probably to
other soluble secretory cargo in the ER, after which the Erv29-cargo
complexes are packaged into COPII vesicles for transport to the Golgi
complex. The authors noted that similar mechanisms have been postulated
for ERGIC1 (LMAN1; 601567).
GENE STRUCTURE
Duhig et al. (1998) stated that the 5-prime end of each of the surfeit
genes, including SURF4, is contained within a CpG island. Although the
mouse Surf2 (185630) and Surf4 genes overlap at their 3-prime ends,
human SURF2 and SURF4 are separated by 302 bp due to a much shorter
3-prime UTR in the human SURF2 gene.
MAPPING
By contig analysis, Duhig et al. (1998) mapped the SURF4 gene to the
telomeric end of the surfeit locus on chromosome 9q34.
*FIELD* RF
1. Belden, W. J.; Barlowe, C.: Role of Erv29p in collecting soluble
secretory proteins into ER-derived transport vesicles. Science 294:
1528-1531, 2001.
2. Duhig, T.; Ruhrberg, C.; Mor, O.; Fried, M.: The human surfeit
locus. Genomics 52: 72-78, 1998.
3. Garson, K.; Duhig, T.; Fried, M.: Tissue-specific processing of
the Surf-5 and Surf-4 mRNAs. Gene Expr. 6: 209-218, 1996.
4. Reeves, J. E.; Fried, M.: The surf-4 gene encodes a novel 30 kDa
integral membrane protein. Molec. Membr. Biol. 12: 201-208, 1995.
*FIELD* CN
Patricia A. Hartz - updated: 11/10/2008
Paul J. Converse - updated: 11/28/2001
*FIELD* CD
Victor A. McKusick: 8/29/1989
*FIELD* ED
mgross: 12/05/2008
terry: 11/10/2008
terry: 7/26/2006
mgross: 11/28/2001
dkim: 7/16/1998
supermim: 3/16/1992
supermim: 3/20/1990
supermim: 2/20/1990
ddp: 10/27/1989
root: 8/29/1989