SCFD1_MOUSE
ID SCFD1_MOUSE Reviewed; 639 AA.
AC Q8BRF7; Q8BRZ2; Q8K179; Q9CXR8;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Sec1 family domain-containing protein 1;
DE AltName: Full=Syntaxin-binding protein 1-like 2;
GN Name=Scfd1; Synonyms=Stxbp1l2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Aorta, Embryo, and Vein;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-597 (ISOFORM 3).
RC TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- 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=Q8BRF7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BRF7-2; Sequence=VSP_011310, VSP_011311;
CC Name=3;
CC IsoId=Q8BRF7-3; Sequence=VSP_011312, VSP_011313;
CC -!- SIMILARITY: Belongs to the STXBP/unc-18/SEC1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH27793.1; 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; AK014070; BAB29141.1; -; mRNA.
DR EMBL; AK041028; BAC30788.1; -; mRNA.
DR EMBL; AK044943; BAC32152.1; -; mRNA.
DR EMBL; BC027793; AAH27793.1; ALT_INIT; mRNA.
DR CCDS; CCDS36439.1; -. [Q8BRF7-1]
DR CCDS; CCDS88336.1; -. [Q8BRF7-2]
DR RefSeq; NP_001293107.1; NM_001306178.1. [Q8BRF7-2]
DR RefSeq; NP_084101.1; NM_029825.3. [Q8BRF7-1]
DR AlphaFoldDB; Q8BRF7; -.
DR SMR; Q8BRF7; -.
DR BioGRID; 218443; 9.
DR STRING; 10090.ENSMUSP00000021335; -.
DR iPTMnet; Q8BRF7; -.
DR PhosphoSitePlus; Q8BRF7; -.
DR EPD; Q8BRF7; -.
DR jPOST; Q8BRF7; -.
DR MaxQB; Q8BRF7; -.
DR PaxDb; Q8BRF7; -.
DR PeptideAtlas; Q8BRF7; -.
DR PRIDE; Q8BRF7; -.
DR ProteomicsDB; 256741; -. [Q8BRF7-1]
DR ProteomicsDB; 256742; -. [Q8BRF7-2]
DR ProteomicsDB; 256743; -. [Q8BRF7-3]
DR Antibodypedia; 112; 371 antibodies from 27 providers.
DR DNASU; 76983; -.
DR Ensembl; ENSMUST00000021335; ENSMUSP00000021335; ENSMUSG00000020952. [Q8BRF7-1]
DR Ensembl; ENSMUST00000219434; ENSMUSP00000151347; ENSMUSG00000020952. [Q8BRF7-2]
DR GeneID; 76983; -.
DR KEGG; mmu:76983; -.
DR UCSC; uc007nmo.1; mouse. [Q8BRF7-2]
DR UCSC; uc007nmq.1; mouse. [Q8BRF7-1]
DR CTD; 23256; -.
DR MGI; MGI:1924233; Scfd1.
DR VEuPathDB; HostDB:ENSMUSG00000020952; -.
DR eggNOG; KOG1301; Eukaryota.
DR GeneTree; ENSGT00550000074845; -.
DR HOGENOM; CLU_016216_3_1_1; -.
DR InParanoid; Q8BRF7; -.
DR OMA; DRQLDNF; -.
DR OrthoDB; 917326at2759; -.
DR PhylomeDB; Q8BRF7; -.
DR TreeFam; TF105740; -.
DR Reactome; R-MMU-204005; COPII-mediated vesicle transport.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR BioGRID-ORCS; 76983; 20 hits in 71 CRISPR screens.
DR PRO; PR:Q8BRF7; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8BRF7; protein.
DR Bgee; ENSMUSG00000020952; Expressed in seminal vesicle and 254 other tissues.
DR ExpressionAtlas; Q8BRF7; baseline and differential.
DR Genevisible; Q8BRF7; MM.
DR GO; GO:0005801; C:cis-Golgi network; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0019905; F:syntaxin binding; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; ISO:MGI.
DR GO; GO:0060628; P:regulation of ER to Golgi vesicle-mediated transport; ISO:MGI.
DR GO; GO:0051223; P:regulation of protein transport; ISO:MGI.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; ISO:MGI.
DR GO; GO:1901998; P:toxin transport; IMP:MGI.
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 Alternative splicing; Cytoplasm; Endoplasmic reticulum; ER-Golgi transport;
KW Golgi apparatus; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..639
FT /note="Sec1 family domain-containing protein 1"
FT /id="PRO_0000206288"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62991"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 525
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVM8"
FT VAR_SEQ 385..390
FT /note="SLPELL -> ALMSVH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011310"
FT VAR_SEQ 391..639
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011311"
FT VAR_SEQ 578..597
FT /note="VPRNKSPFQEAIVFVVGGGN -> FLYKTEEPPASQEGGPGIPS (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011312"
FT VAR_SEQ 598..639
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011313"
FT CONFLICT 328
FT /note="G -> E (in Ref. 1; BAB29141)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 639 AA; 72323 MW; D7058563F8549322 CRC64;
MVGSKMAATA SIRERQTVAL KRMLNFNVPH VKNSTGEPVW KVLIYDRFGQ DIISPLLSVK
ELRDMGITLH LLLHSDRDPI PDVPAVYFVM PTEENIDRLC QDLRNQLYES YYLNFISAIS
RSKLEDIANA ALAASAVTQV AKVFDQYLNF ITLEDDMFVL CNQNKELVSY RAINRPDITD
TEMETVMDTI VDSLFCFFVT LGAVPIIRCS RGTAAEMVAV KLDKKLRENL RDARNSLFTG
DPLGTGQFSF QRPLLVLVDR NIDLATPLHH TWTYQALVHD VLDFHLNRVN LEESTGVENS
PAGARPKRKN KKSYDLTPVD KFWQKHKGSP FPEVAESVQQ ELESYRAQED EVKRLKSIMG
LEGEDEGAIS MLSDNTAKLT SAVSSLPELL EKKRLIDLHT NVATAVLEHI KARKLDVYFE
YEEKIMSKTT LDKSLLDVIS DPDAGTPEDK MRLFLIYYIS AQQAPSEVDL EQYKKALTDA
GCNLSPLQYI KQWKAFAKMA STPASYGNTT TKPMGLLSRV MNTGSQFVME GVKNLVLKQQ
NLPVTRILDN LMEMKSNPET DDYRYFDPKM LRSNDSSVPR NKSPFQEAIV FVVGGGNYIE
YQNLVDYIKA KQGKHILYGC SEIFNATQFI KQLSQLGQK
