SCFD1_HUMAN
ID SCFD1_HUMAN Reviewed; 642 AA.
AC Q8WVM8; A8K2Z5; B7Z4U7; B7Z594; O60754; O94990; Q7Z529; Q9BZI3; Q9UNL3;
AC Q9Y6A8;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Sec1 family domain-containing protein 1;
DE AltName: Full=SLY1 homolog;
DE Short=Sly1p;
DE AltName: Full=Syntaxin-binding protein 1-like 2;
GN Name=SCFD1; Synonyms=C14orf163, KIAA0917, STXBP1L2; ORFNames=FKSG23;
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] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Pituitary;
RA Song H., Peng Y., Dai M., Huang Q., Mao Y., Zhang Q., Mao M., Fu G.,
RA Luo M., Chen J., Hu R.;
RT "Human vesicle transport-related protein gene.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Wang Y.-G., Gong L.;
RT "Identification of FKSG23, a vesicle transport-related protein.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Dai F.Y., Yu L., Ding J.B., Lin W., Yang Y.M., Zhao S.Y.;
RT "Cloning of a novel human cDNA homology to R.norvegicus rsly1p mRNA.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT
RP ARG-63.
RC TISSUE=Heart, and Umbilical cord blood;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-63.
RC TISSUE=Lymph;
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 [9]
RP PROTEIN SEQUENCE OF 2-16.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [10]
RP PROTEIN SEQUENCE OF 2-16; 125-145; 382-395 AND 502-536, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Foreskin fibroblast, and Prostatic carcinoma;
RA Bienvenut W.V., Gao M., Leug H., Campbell A., Ozanne B.W.;
RL Submitted (JUL-2009) to UniProtKB.
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 572-642.
RC TISSUE=Placenta;
RA Page N.M., Butlin D.J., Manyonda I., Bicknell A.B., Lowry P.J.;
RT "Differential display of placental genes.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
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 [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303 AND SER-528, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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).
CC -!- FUNCTION: Plays a role in SNARE-pin assembly and Golgi-to-ER retrograde
CC transport via its interaction with COG4. Involved in vesicular
CC transport between the endoplasmic reticulum and the Golgi (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with STX17. Interacts with STX5A. Interacts with the
CC COG complex via COG4 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q8WVM8; Q9H9E3: COG4; NbExp=10; IntAct=EBI-722569, EBI-368382;
CC Q8WVM8; P42858: HTT; NbExp=3; IntAct=EBI-722569, EBI-466029;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endoplasmic reticulum
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC Golgi apparatus, Golgi stack membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8WVM8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WVM8-2; Sequence=VSP_047070;
CC Name=3;
CC IsoId=Q8WVM8-3; Sequence=VSP_047071;
CC -!- SIMILARITY: Belongs to the STXBP/unc-18/SEC1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD40381.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAD48586.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAP97146.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA74940.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB020724; BAA74940.2; ALT_INIT; mRNA.
DR EMBL; AF092139; AAD40381.1; ALT_FRAME; mRNA.
DR EMBL; AF110646; AAD48586.1; ALT_FRAME; mRNA.
DR EMBL; AF319958; AAG50273.1; -; mRNA.
DR EMBL; AF086916; AAP97146.1; ALT_FRAME; mRNA.
DR EMBL; AK290410; BAF83099.1; -; mRNA.
DR EMBL; AK298622; BAH12830.1; -; mRNA.
DR EMBL; AK297873; BAH12683.1; -; mRNA.
DR EMBL; AK316212; BAH14583.1; -; mRNA.
DR EMBL; AL121852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471078; EAW65968.1; -; Genomic_DNA.
DR EMBL; BC017734; AAH17734.1; -; mRNA.
DR EMBL; AF067205; AAC17907.1; -; mRNA.
DR CCDS; CCDS45092.1; -. [Q8WVM8-3]
DR CCDS; CCDS58308.1; -. [Q8WVM8-2]
DR CCDS; CCDS9639.1; -. [Q8WVM8-1]
DR RefSeq; NP_001244305.1; NM_001257376.1. [Q8WVM8-2]
DR RefSeq; NP_001269961.1; NM_001283032.1.
DR RefSeq; NP_057190.2; NM_016106.3. [Q8WVM8-1]
DR RefSeq; NP_878255.1; NM_182835.2. [Q8WVM8-3]
DR AlphaFoldDB; Q8WVM8; -.
DR SMR; Q8WVM8; -.
DR BioGRID; 116860; 186.
DR IntAct; Q8WVM8; 52.
DR MINT; Q8WVM8; -.
DR STRING; 9606.ENSP00000390783; -.
DR GlyGen; Q8WVM8; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q8WVM8; -.
DR MetOSite; Q8WVM8; -.
DR PhosphoSitePlus; Q8WVM8; -.
DR SwissPalm; Q8WVM8; -.
DR BioMuta; SCFD1; -.
DR DMDM; 51316882; -.
DR EPD; Q8WVM8; -.
DR jPOST; Q8WVM8; -.
DR MassIVE; Q8WVM8; -.
DR MaxQB; Q8WVM8; -.
DR PaxDb; Q8WVM8; -.
DR PeptideAtlas; Q8WVM8; -.
DR PRIDE; Q8WVM8; -.
DR ProteomicsDB; 6636; -.
DR ProteomicsDB; 6669; -.
DR ProteomicsDB; 74805; -. [Q8WVM8-1]
DR Antibodypedia; 112; 371 antibodies from 27 providers.
DR DNASU; 23256; -.
DR Ensembl; ENST00000396629.6; ENSP00000379870.2; ENSG00000092108.22. [Q8WVM8-2]
DR Ensembl; ENST00000458591.7; ENSP00000390783.2; ENSG00000092108.22. [Q8WVM8-1]
DR Ensembl; ENST00000544052.6; ENSP00000443010.2; ENSG00000092108.22. [Q8WVM8-3]
DR Ensembl; ENST00000678124.1; ENSP00000503029.1; ENSG00000092108.22. [Q8WVM8-3]
DR GeneID; 23256; -.
DR KEGG; hsa:23256; -.
DR MANE-Select; ENST00000458591.7; ENSP00000390783.2; NM_016106.4; NP_057190.2.
DR UCSC; uc001wqm.3; human. [Q8WVM8-1]
DR CTD; 23256; -.
DR DisGeNET; 23256; -.
DR GeneCards; SCFD1; -.
DR HGNC; HGNC:20726; SCFD1.
DR HPA; ENSG00000092108; Low tissue specificity.
DR MIM; 618207; gene.
DR neXtProt; NX_Q8WVM8; -.
DR OpenTargets; ENSG00000092108; -.
DR PharmGKB; PA134946073; -.
DR VEuPathDB; HostDB:ENSG00000092108; -.
DR eggNOG; KOG1301; Eukaryota.
DR GeneTree; ENSGT00550000074845; -.
DR HOGENOM; CLU_016216_3_1_1; -.
DR InParanoid; Q8WVM8; -.
DR OMA; DRQLDNF; -.
DR OrthoDB; 917326at2759; -.
DR PhylomeDB; Q8WVM8; -.
DR TreeFam; TF105740; -.
DR PathwayCommons; Q8WVM8; -.
DR Reactome; R-HSA-204005; COPII-mediated vesicle transport.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR SignaLink; Q8WVM8; -.
DR BioGRID-ORCS; 23256; 733 hits in 1080 CRISPR screens.
DR ChiTaRS; SCFD1; human.
DR GeneWiki; SCFD1; -.
DR GenomeRNAi; 23256; -.
DR Pharos; Q8WVM8; Tbio.
DR PRO; PR:Q8WVM8; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q8WVM8; protein.
DR Bgee; ENSG00000092108; Expressed in calcaneal tendon and 212 other tissues.
DR ExpressionAtlas; Q8WVM8; baseline and differential.
DR Genevisible; Q8WVM8; HS.
DR GO; GO:0005801; C:cis-Golgi network; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0005798; C:Golgi-associated vesicle; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
DR GO; GO:0044877; F:protein-containing complex binding; ISS:UniProtKB.
DR GO; GO:0019905; F:syntaxin binding; ISS:UniProtKB.
DR GO; GO:0000902; P:cell morphogenesis; ISS:ParkinsonsUK-UCL.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:1902902; P:negative regulation of autophagosome assembly; IMP:UniProtKB.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; ISS:UniProtKB.
DR GO; GO:0060628; P:regulation of ER to Golgi vesicle-mediated transport; ISS:UniProtKB.
DR GO; GO:0051223; P:regulation of protein transport; IMP:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0009636; P:response to toxic substance; IEP:UniProtKB.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:1901998; P:toxin transport; IEA:Ensembl.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 3.40.50.1910; -; 1.
DR Gene3D; 3.40.50.2060; -; 1.
DR Gene3D; 3.90.830.10; -; 1.
DR InterPro; IPR043154; Sec-1-like_dom1.
DR InterPro; IPR043127; Sec-1-like_dom3a.
DR InterPro; IPR001619; Sec1-like.
DR InterPro; IPR027482; Sec1-like_dom2.
DR InterPro; IPR036045; Sec1-like_sf.
DR PANTHER; PTHR11679; PTHR11679; 1.
DR Pfam; PF00995; Sec1; 1.
DR PIRSF; PIRSF005715; VPS45_Sec1; 1.
DR SUPFAM; SSF56815; SSF56815; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801, ECO:0000269|Ref.10,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT CHAIN 2..642
FT /note="Sec1 family domain-containing protein 1"
FT /id="PRO_0000206287"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.10, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62991"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..92
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047070"
FT VAR_SEQ 1..67
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047071"
FT VARIANT 63
FT /note="K -> R (in dbSNP:rs229150)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_019616"
FT CONFLICT 42
FT /note="V -> I (in Ref. 3; AAG50273)"
FT /evidence="ECO:0000305"
FT CONFLICT 136..137
FT /note="AA -> EL (in Ref. 2; AAD40381)"
FT /evidence="ECO:0000305"
FT CONFLICT 201..206
FT /note="FVTLGA -> YGTRGD (in Ref. 2; AAD48586)"
FT /evidence="ECO:0000305"
FT CONFLICT 201..202
FT /note="FV -> YG (in Ref. 2; AAD40381 and 4; AAP97146)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="A -> D (in Ref. 4; AAP97146)"
FT /evidence="ECO:0000305"
FT CONFLICT 453
FT /note="K -> N (in Ref. 2; AAD48586)"
FT /evidence="ECO:0000305"
FT CONFLICT 484..485
FT /note="GC -> EM (in Ref. 2; AAD40381)"
FT /evidence="ECO:0000305"
FT CONFLICT 485
FT /note="Missing (in Ref. 2; AAD48586)"
FT /evidence="ECO:0000305"
FT CONFLICT 562..563
FT /note="ET -> KL (in Ref. 2; AAD40381)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 642 AA; 72380 MW; 0340FB9F05CD24CE CRC64;
MAAAAAATAA AAASIRERQT VALKRMLNFN VPHIKNSTGE PVWKVLIYDR FGQDIISPLL
SVKELRDMGI TLHLLLHSDR DPIPDVPAVY FVMPTEENID RMCQDLRNQL YESYYLNFIS
AISRSKLEDI ANAALAASAV TQVAKVFDQY LNFITLEDDM FVLCNQNKEL VSYRAINRPD
ITDTEMETVM DTIVDSLFCF FVTLGAVPII RCSRGTAAEM VAVKLDKKLR ENLRDARNSL
FTGDTLGAGQ FSFQRPLLVL VDRNIDLATP LHHTWTYQAL VHDVLDFHLN RVNLEESSGV
ENSPAGARPK RKNKKSYDLT PVDKFWQKHK GSPFPEVAES VQQELESYRA QEDEVKRLKS
IMGLEGEDEG AISMLSDNTA KLTSAVSSLP ELLEKKRLID LHTNVATAVL EHIKARKLDV
YFEYEEKIMS KTTLDKSLLD IISDPDAGTP EDKMRLFLIY YISTQQAPSE ADLEQYKKAL
TDAGCNLNPL QYIKQWKAFT KMASAPASYG STTTKPMGLL SRVMNTGSQF VMEGVKNLVL
KQQNLPVTRI LDNLMEMKSN PETDDYRYFD PKMLRGNDSS VPRNKNPFQE AIVFVVGGGN
YIEYQNLVDY IKGKQGKHIL YGCSELFNAT QFIKQLSQLG QK
