SCFD1_RAT
ID SCFD1_RAT Reviewed; 637 AA.
AC Q62991; Q62843;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 145.
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;
DE AltName: Full=Vesicle transport-related protein Ra410;
GN Name=Scfd1; Synonyms=Ra410, Sly1, Stxbp1l2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-30; 81-92; 211-219 AND
RP 554-561, FUNCTION, AND INTERACTION WITH STX5A.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8663406; DOI=10.1074/jbc.271.27.15866;
RA Dascher C., Balch W.E.;
RT "Mammalian Sly1 regulates syntaxin 5 function in endoplasmic reticulum to
RT Golgi transport.";
RL J. Biol. Chem. 271:15866-15869(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=9195952; DOI=10.1074/jbc.272.26.16438;
RA Matsuo N., Ogawa S., Takagi T., Wanaka A., Mori T., Matsuyama T.,
RA Pinsky D.J., Stern D.M., Tohyama M.;
RT "Cloning of a putative vesicle transport-related protein, RA410, from
RT cultured rat astrocytes and its expression in ischemic rat brain.";
RL J. Biol. Chem. 272:16438-16444(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-637, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=8647468; DOI=10.1016/0378-1119(95)00819-5;
RA Peterson M.R., Hsu S.C., Scheller R.H.;
RT "A mammalian homologue of SLY1, a yeast gene required for transport from
RT endoplasmic reticulum to Golgi.";
RL Gene 169:293-294(1996).
RN [4]
RP INTERACTION WITH STX17.
RX PubMed=10930465; DOI=10.1091/mbc.11.8.2719;
RA Steegmaier M., Oorschot V., Klumperman J., Scheller R.H.;
RT "Syntaxin 17 is abundant in steroidogenic cells and implicated in smooth
RT endoplasmic reticulum membrane dynamics.";
RL Mol. Biol. Cell 11:2719-2731(2000).
RN [5]
RP FUNCTION, AND INTERACTION WITH COG4.
RX PubMed=19536132; DOI=10.1038/emboj.2009.168;
RA Laufman O., Kedan A., Hong W., Lev S.;
RT "Direct interaction between the COG complex and the SM protein, Sly1, is
RT required for Golgi SNARE pairing.";
RL EMBO J. 28:2006-2017(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32 AND SER-298, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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.
CC {ECO:0000269|PubMed:19536132, ECO:0000269|PubMed:8663406,
CC ECO:0000269|PubMed:9195952}.
CC -!- SUBUNIT: Interacts with STX17 (Probable). Interacts with the COG
CC complex via COG4. Interacts with STX5A. {ECO:0000269|PubMed:10930465,
CC ECO:0000269|PubMed:19536132, ECO:0000269|PubMed:8663406, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9195952}.
CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:9195952}; Peripheral
CC membrane protein {ECO:0000269|PubMed:9195952}. Golgi apparatus, Golgi
CC stack membrane {ECO:0000269|PubMed:9195952}; Peripheral membrane
CC protein {ECO:0000269|PubMed:9195952}.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis. Detected at lower
CC levels in brain, astrocytes, heart and small intestine.
CC {ECO:0000269|PubMed:8647468, ECO:0000269|PubMed:9195952}.
CC -!- INDUCTION: Up-regulated in astrocytes upon reoxygenation after hypoxia.
CC {ECO:0000269|PubMed:9195952}.
CC -!- SIMILARITY: Belongs to the STXBP/unc-18/SEC1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB08009.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U57687; AAC52636.1; -; mRNA.
DR EMBL; D79221; BAA24276.1; -; mRNA.
DR EMBL; U35364; AAB08009.1; ALT_INIT; mRNA.
DR PIR; JC4674; JC4674.
DR RefSeq; NP_062237.1; NM_019364.1.
DR PDB; 1Y9J; NMR; -; A=2-147.
DR PDBsum; 1Y9J; -.
DR AlphaFoldDB; Q62991; -.
DR SMR; Q62991; -.
DR BioGRID; 248542; 1.
DR CORUM; Q62991; -.
DR IntAct; Q62991; 3.
DR STRING; 10116.ENSRNOP00000039132; -.
DR iPTMnet; Q62991; -.
DR PhosphoSitePlus; Q62991; -.
DR jPOST; Q62991; -.
DR PaxDb; Q62991; -.
DR PRIDE; Q62991; -.
DR Ensembl; ENSRNOT00000040548; ENSRNOP00000039132; ENSRNOG00000031203.
DR GeneID; 54350; -.
DR KEGG; rno:54350; -.
DR UCSC; RGD:619828; rat.
DR CTD; 23256; -.
DR RGD; 619828; Scfd1.
DR eggNOG; KOG1301; Eukaryota.
DR GeneTree; ENSGT00550000074845; -.
DR HOGENOM; CLU_016216_3_1_1; -.
DR InParanoid; Q62991; -.
DR OMA; DRQLDNF; -.
DR OrthoDB; 917326at2759; -.
DR PhylomeDB; Q62991; -.
DR TreeFam; TF105740; -.
DR Reactome; R-RNO-204005; COPII-mediated vesicle transport.
DR Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR EvolutionaryTrace; Q62991; -.
DR PRO; PR:Q62991; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000031203; Expressed in jejunum and 20 other tissues.
DR Genevisible; Q62991; RN.
DR GO; GO:0005801; C:cis-Golgi network; ISO:RGD.
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; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR GO; GO:0019905; F:syntaxin binding; IDA:RGD.
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:RGD.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; IDA:RGD.
DR GO; GO:0060628; P:regulation of ER to Golgi vesicle-mediated transport; IMP:RGD.
DR GO; GO:0051223; P:regulation of protein transport; ISO:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0009636; P:response to toxic substance; ISO:RGD.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IMP:UniProtKB.
DR GO; GO:1901998; P:toxin transport; ISO:RGD.
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 3D-structure; Cytoplasm; Direct protein sequencing; Endoplasmic reticulum;
KW ER-Golgi transport; Golgi apparatus; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..637
FT /note="Sec1 family domain-containing protein 1"
FT /id="PRO_0000206289"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVM8"
FT HELIX 9..21
FT /evidence="ECO:0007829|PDB:1Y9J"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:1Y9J"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:1Y9J"
FT HELIX 45..51
FT /evidence="ECO:0007829|PDB:1Y9J"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:1Y9J"
FT HELIX 57..62
FT /evidence="ECO:0007829|PDB:1Y9J"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:1Y9J"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:1Y9J"
FT HELIX 91..103
FT /evidence="ECO:0007829|PDB:1Y9J"
FT STRAND 106..115
FT /evidence="ECO:0007829|PDB:1Y9J"
FT HELIX 119..130
FT /evidence="ECO:0007829|PDB:1Y9J"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:1Y9J"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:1Y9J"
SQ SEQUENCE 637 AA; 72263 MW; 9ABFBBEBD2862341 CRC64;
MVGSKMAASI RERQTVALKR MLNFNVPHVK NSPGEPVWKV LIYDRFGQDI ISPLLSVKEL
RDMGITLHLL LHSDRDPIRD VPAVYFVMPT EENIDRLCQD LRNQLYESYY LNFISAISRS
KLEDIANAAL AANAVTQVAK VFDQYLNFIT LEEDMFVLCN QNKELVSYRA INRPDITDTE
METVMDTIVD SLFCFFVTLG AVPIIRCSRG TAAEMVAVKL DKKLRENLRD ARNSLFTGDP
LGTGQFSFQR PLLVLVDRNI DLATPLHHTW TYQALVHDVL DFHLNRVNLE ESTGVENSPT
GARPKRKNKK SYDLTPVDKF WQKHKGSPFP EVAESVQQEL ESYRAQEDEV KRLKSIMGLE
GEDEGAISML SDNTAKLTSA VSSLPELLEK KRLIDLHTNV ATAVLEHIKA RKLDVYFEYE
EKIMSKTTLD KSLLDVISDP DAGTPEDKMR LFLIYYISAQ QAPSEVDLEQ YKKALTDAGC
NLSPLQYIKQ WKAFAKMAST PASYGNTTTK PMGLLSRVMN TGSQFVMEGV KNLVLKQQNL
PVTRILDNLM EMKSNPETDD YRYFDPKMLR SNDSSVPRNK SPFQEAIVFV VGGGNYIEYQ
NLVDYIKGKQ GKHILYGCSE IFNATQFIKQ LSQLGQK
