MSS4_RAT
ID MSS4_RAT Reviewed; 123 AA.
AC Q08326;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Guanine nucleotide exchange factor MSS4;
DE AltName: Full=Rab-interacting factor;
GN Name=Rabif; Synonyms=Mss4;
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].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=8429887; DOI=10.1038/361464a0;
RA Burton J., Roberts D., Montaldi M., Novick P., de Camilli P.;
RT "A mammalian guanine-nucleotide-releasing protein enhances function of
RT yeast secretory protein Sec4.";
RL Nature 361:464-467(1993).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 9-123, AND ZINC-BINDING SITES.
RX PubMed=11258916; DOI=10.1021/bi002680o;
RA Zhu Z., Dumas J.J., Lietzke S.E., Lambright D.G.;
RT "A helical turn motif in Mss4 is a critical determinant of Rab binding and
RT nucleotide release.";
RL Biochemistry 40:3027-3036(2001).
CC -!- FUNCTION: Guanine-nucleotide-releasing protein that acts on members of
CC the SEC4/YPT1/RAB subfamily. Stimulates GDP release from both YPT1,
CC RAB3A and RAB10, but is less active on these proteins than on the SEC4
CC protein. Might play a general role in vesicular transport.
CC {ECO:0000250|UniProtKB:P47224}.
CC -!- SUBUNIT: Interacts with RAB8A. {ECO:0000250|UniProtKB:P47224}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the DSS4/MSS4 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01132}.
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DR EMBL; X70496; CAA49904.1; -; mRNA.
DR PIR; S29714; S29714.
DR RefSeq; NP_001007679.1; NM_001007678.2.
DR RefSeq; XP_003749349.1; XM_003749301.4.
DR PDB; 1HXR; X-ray; 1.65 A; A/B=9-123.
DR PDBsum; 1HXR; -.
DR AlphaFoldDB; Q08326; -.
DR SMR; Q08326; -.
DR BioGRID; 257986; 1.
DR STRING; 10116.ENSRNOP00000005845; -.
DR PaxDb; Q08326; -.
DR PRIDE; Q08326; -.
DR Ensembl; ENSRNOT00000005845; ENSRNOP00000005845; ENSRNOG00000004424.
DR GeneID; 304807; -.
DR KEGG; rno:304807; -.
DR UCSC; RGD:1359331; rat.
DR CTD; 5877; -.
DR RGD; 1359331; Rabif.
DR eggNOG; KOG4113; Eukaryota.
DR GeneTree; ENSGT00390000016889; -.
DR HOGENOM; CLU_132754_0_0_1; -.
DR InParanoid; Q08326; -.
DR OMA; WHSLDDK; -.
DR OrthoDB; 1495679at2759; -.
DR PhylomeDB; Q08326; -.
DR TreeFam; TF314029; -.
DR EvolutionaryTrace; Q08326; -.
DR PRO; PR:Q08326; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000004424; Expressed in cerebellum and 19 other tissues.
DR ExpressionAtlas; Q08326; baseline and differential.
DR Genevisible; Q08326; RN.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; ISO:RGD.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR CDD; cd00246; RabGEF; 1.
DR Gene3D; 2.170.150.10; -; 1.
DR InterPro; IPR007515; Mss4.
DR InterPro; IPR011057; Mss4-like_sf.
DR InterPro; IPR011323; Mss4/transl-control_tumour.
DR PANTHER; PTHR13276; PTHR13276; 1.
DR Pfam; PF04421; Mss4; 1.
DR SUPFAM; SSF51316; SSF51316; 1.
DR PROSITE; PS51796; MSS4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Guanine-nucleotide releasing factor;
KW Metal-binding; Protein transport; Reference proteome; Transport; Zinc.
FT CHAIN 1..123
FT /note="Guanine nucleotide exchange factor MSS4"
FT /id="PRO_0000174176"
FT DOMAIN 9..123
FT /note="MSS4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01132"
FT BINDING 23
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01132"
FT BINDING 26
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01132"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01132"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01132"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P47224"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:1HXR"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:1HXR"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:1HXR"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:1HXR"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:1HXR"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:1HXR"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:1HXR"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:1HXR"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:1HXR"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:1HXR"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:1HXR"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:1HXR"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:1HXR"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:1HXR"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:1HXR"
SQ SEQUENCE 123 AA; 13928 MW; ACB7D07E2735811C CRC64;
MEPCELQNEL VSAEGRNRKA VLCQRCGSRV LQPGTALFSR RQLFLPSMRK KPDLVDGSNP
DGDVLEEHWL VNDMFIFENV GFTKDVGNVK FLVCADCEIG PIGWHCLDDK NSFYVALERV
SHE
