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 04-NOV-2026, entry version 198. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_016106.4. [Q8WVM8-1] DR RefSeq; NP_878255.1; NM_182835.2. [Q8WVM8-3] DR SMR; Q8WVM8; -. DR BioGRID; 116860; 308. DR IntAct; Q8WVM8; 160. DR STRING; 9606.ENSP00000390783; -. DR BindingDB; Q8WVM8; -. DR ChEMBL; CHEMBL6067340; -. DR GlyCosmos; Q8WVM8; 3 sites, 1 glycan. DR GlyGen; Q8WVM8; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; Q8WVM8; -. DR PhosphoSitePlus; Q8WVM8; -. DR SwissPalm; Q8WVM8; -. DR MetOSite; Q8WVM8; -. DR BioMuta; SCFD1; -. DR DMDM; 51316882; -. DR PaxDb; 9606-ENSP00000390783; -. DR PeptideAtlas; Q8WVM8; -. DR ProteomicsDB; 6636; -. DR ProteomicsDB; 6669; -. DR ProteomicsDB; 74805; -. [Q8WVM8-1] DR Pumba; Q8WVM8; -. DR jPOST; Q8WVM8; -. DR MassIVE; Q8WVM8; -. DR DNASU; 23256; -. DR Ensembl; ENST00000396629.6; ENSP00000379870.2; ENSG00000092108.23. [Q8WVM8-2] DR Ensembl; ENST00000458591.7; ENSP00000390783.2; ENSG00000092108.23. [Q8WVM8-1] DR Ensembl; ENST00000544052.6; ENSP00000443010.2; ENSG00000092108.23. [Q8WVM8-3] DR Ensembl; ENST00000678124.1; ENSP00000503029.1; ENSG00000092108.23. [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 VEuPathDB; HostDB:ENSG00000092108; -. DR GeneCards; SCFD1; -. DR HGNC; HGNC:20726; SCFD1. DR AGR; HGNC:20726; -. DR HPA; ENSG00000092108; Low tissue specificity. DR MIM; 618207; gene. DR OpenTargets; ENSG00000092108; -. DR ClinPGx; PA134946073; -. DR eggNOG; KOG1301; Eukaryota. DR GeneTree; ENSGT00550000074845; -. DR HOGENOM; CLU_016216_3_1_1; -. DR InParanoid; Q8WVM8; -. DR OMA; AADCSDM; -. DR OrthoDB; 10251230at2759; -. DR PhylomeDB; Q8WVM8; -. DR Reactome; R-HSA-204005; COPII-mediated vesicle transport. DR Reactome; R-HSA-8980692; RHOA GTPase cycle. DR SignaLink; Q8WVM8; -. DR ChiTaRS; SCFD1; human. DR Agora; ENSG00000092108; -. DR GeneWiki; SCFD1; -. DR GenomeRNAi; 23256; -. DR PRO; PR:Q8WVM8; -. DR Bgee; ENSG00000092108; Expressed in calcaneal tendon and 214 other cell types or tissues. DR ExpressionAtlas; Q8WVM8; baseline and differential. DR FunFam; 1.25.40.60:FF:000002; Sec1 family domain containing 1; 1. DR FunFam; 3.40.50.2060:FF:000002; sec1 family domain-containing protein 1; 1. DR Gene3D; 1.25.40.60; -; 1. DR Gene3D; 3.40.50.1910; -; 1. DR Gene3D; 3.40.50.2060; -; 1. DR Gene3D; 3.90.830.10; Syntaxin Binding Protein 1, Chain A, domain 2; 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; VESICLE PROTEIN SORTING-ASSOCIATED; 1. DR Pfam; PF00995; Sec1; 1. DR PIRSF; PIRSF005715; VPS45_Sec1; 1. DR SUPFAM; SSF56815; Sec1/munc18-like (SM) proteins; 1. 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:0044877; F:protein-containing complex binding; ISS:UniProtKB. DR GO; GO:0019905; F:syntaxin binding; ISS:UniProtKB. 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:0009636; P:response to toxic substance; IEP:UniProtKB. DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; ISS:UniProtKB. DR Proteomes; UP000005640; Chromosome 14. DR PathwayCommons; Q8WVM8; -. DR Pharos; Q8WVM8; Tbio. DR Antibodypedia; 112; 409 antibodies from 30 providers. DR RNAct; Q8WVM8; protein. DR BioGRID-ORCS; 23256; 759 hits in 1158 CRISPR screens. DR AlphaFoldDB; Q8WVM8; -. DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities. DR FunCoup; Q8WVM8; 4016. DR PAN-GO; Q8WVM8; 5 GO annotations based on evolutionary models. 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; Proteomics identification; KW 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 //