MSS4_HUMAN
ID MSS4_HUMAN Reviewed; 123 AA.
AC P47224; B2R4P4; Q92992;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Guanine nucleotide exchange factor MSS4;
DE AltName: Full=Rab-interacting factor;
GN Name=RABIF; Synonyms=MSS4, RASGRF3;
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 [MRNA].
RC TISSUE=Brain;
RX PubMed=7619808; DOI=10.1021/bi00028a020;
RA Yu H., Schreiber S.L.;
RT "Cloning, Zn2+ binding, and structural characterization of the guanine
RT nucleotide exchange factor human Mss4.";
RL Biochemistry 34:9103-9110(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9441742; DOI=10.1006/geno.1997.5049;
RA Mueller-Pillasch F., Zimmerhackl F., Lacher U., Schultz N., Hameister H.,
RA Varga G., Friess H., Buechler M., Adler G., Gress T.M.;
RT "Cloning of novel transcripts of the human guanine-nucleotide-exchange
RT factor Mss4: in situ chromosomal mapping and expression in pancreatic
RT cancer.";
RL Genomics 46:389-396(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Prostate;
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 [7]
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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [10]
RP FUNCTION.
RX PubMed=31540829; DOI=10.1016/j.chom.2019.08.017;
RA Jeng E.E., Bhadkamkar V., Ibe N.U., Gause H., Jiang L., Chan J., Jian R.,
RA Jimenez-Morales D., Stevenson E., Krogan N.J., Swaney D.L., Snyder M.P.,
RA Mukherjee S., Bassik M.C.;
RT "Systematic Identification of Host Cell Regulators of Legionella
RT pneumophila Pathogenesis Using a Genome-wide CRISPR Screen.";
RL Cell Host Microbe 26:551.E6-563.E6(2019).
RN [11]
RP STRUCTURE BY NMR.
RX PubMed=7651540; DOI=10.1038/376788a0;
RA Yu H., Schreiber S.L.;
RT "Structure of guanine-nucleotide-exchange factor human Mss4 and
RT identification of its Rab-interacting surface.";
RL Nature 376:788-791(1995).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 11-123 IN COMPLEX WITH RAB8A, AND
RP INTERACTION WITH RAB8A.
RX PubMed=16541104; DOI=10.1038/sj.emboj.7601044;
RA Itzen A., Pylypenko O., Goody R.S., Alexandrov K., Rak A.;
RT "Nucleotide exchange via local protein unfolding--structure of Rab8 in
RT complex with MSS4.";
RL EMBO J. 25:1445-1455(2006).
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 (PubMed:31540829). Might play a general role in vesicular
CC transport. {ECO:0000269|PubMed:31540829}.
CC -!- SUBUNIT: Interacts with RAB8A. {ECO:0000269|PubMed:16541104}.
CC -!- INTERACTION:
CC P47224; O00303: EIF3F; NbExp=5; IntAct=EBI-713992, EBI-711990;
CC P47224; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-713992, EBI-14069005;
CC P47224; Q659C4-6: LARP1B; NbExp=3; IntAct=EBI-713992, EBI-12036449;
CC P47224; Q9NZU5: LMCD1; NbExp=3; IntAct=EBI-713992, EBI-5774016;
CC P47224; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-713992, EBI-739832;
CC P47224; A0A087WWI0: LRMDA; NbExp=3; IntAct=EBI-713992, EBI-18393842;
CC P47224; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-713992, EBI-1216080;
CC P47224; A4D1S5: RAB19; NbExp=5; IntAct=EBI-713992, EBI-4401710;
CC P47224; P62820: RAB1A; NbExp=3; IntAct=EBI-713992, EBI-716845;
CC P47224; Q9H0U4: RAB1B; NbExp=7; IntAct=EBI-713992, EBI-1045214;
CC P47224; P20336: RAB3A; NbExp=9; IntAct=EBI-713992, EBI-1045943;
CC P47224; P20337: RAB3B; NbExp=5; IntAct=EBI-713992, EBI-12894629;
CC P47224; Q96E17: RAB3C; NbExp=5; IntAct=EBI-713992, EBI-4287022;
CC P47224; O95716: RAB3D; NbExp=3; IntAct=EBI-713992, EBI-3386067;
CC P47224; P61006: RAB8A; NbExp=6; IntAct=EBI-713992, EBI-722293;
CC P47224; Q8WWW0: RASSF5; NbExp=3; IntAct=EBI-713992, EBI-367390;
CC P47224; Q04864: REL; NbExp=3; IntAct=EBI-713992, EBI-307352;
CC P47224; P15884: TCF4; NbExp=3; IntAct=EBI-713992, EBI-533224;
CC P47224; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-713992, EBI-750109;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the DSS4/MSS4 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01132}.
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DR EMBL; S78873; AAB34955.1; -; mRNA.
DR EMBL; U74324; AAB18264.1; -; mRNA.
DR EMBL; BT007133; AAP35797.1; -; mRNA.
DR EMBL; AK311900; BAG34841.1; -; mRNA.
DR EMBL; CH471067; EAW91443.1; -; Genomic_DNA.
DR EMBL; BC018488; AAH18488.1; -; mRNA.
DR EMBL; BC037392; AAH37392.1; -; mRNA.
DR CCDS; CCDS1428.1; -.
DR PIR; I52427; I52427.
DR RefSeq; NP_002862.2; NM_002871.4.
DR PDB; 1FWQ; NMR; -; A=1-123.
DR PDB; 2FU5; X-ray; 2.00 A; A/B=11-123.
DR PDBsum; 1FWQ; -.
DR PDBsum; 2FU5; -.
DR AlphaFoldDB; P47224; -.
DR SMR; P47224; -.
DR BioGRID; 111815; 75.
DR IntAct; P47224; 28.
DR MINT; P47224; -.
DR STRING; 9606.ENSP00000356231; -.
DR iPTMnet; P47224; -.
DR PhosphoSitePlus; P47224; -.
DR BioMuta; RABIF; -.
DR EPD; P47224; -.
DR jPOST; P47224; -.
DR MassIVE; P47224; -.
DR MaxQB; P47224; -.
DR PaxDb; P47224; -.
DR PeptideAtlas; P47224; -.
DR PRIDE; P47224; -.
DR ProteomicsDB; 55784; -.
DR TopDownProteomics; P47224; -.
DR Antibodypedia; 34532; 112 antibodies from 26 providers.
DR DNASU; 5877; -.
DR Ensembl; ENST00000367262.4; ENSP00000356231.3; ENSG00000183155.5.
DR GeneID; 5877; -.
DR KEGG; hsa:5877; -.
DR MANE-Select; ENST00000367262.4; ENSP00000356231.3; NM_002871.5; NP_002862.2.
DR UCSC; uc001gyl.4; human.
DR CTD; 5877; -.
DR DisGeNET; 5877; -.
DR GeneCards; RABIF; -.
DR HGNC; HGNC:9797; RABIF.
DR HPA; ENSG00000183155; Low tissue specificity.
DR MIM; 603417; gene.
DR neXtProt; NX_P47224; -.
DR OpenTargets; ENSG00000183155; -.
DR PharmGKB; PA34158; -.
DR VEuPathDB; HostDB:ENSG00000183155; -.
DR eggNOG; KOG4113; Eukaryota.
DR GeneTree; ENSGT00390000016889; -.
DR HOGENOM; CLU_132754_0_0_1; -.
DR InParanoid; P47224; -.
DR OMA; WHSLDDK; -.
DR OrthoDB; 1495679at2759; -.
DR PhylomeDB; P47224; -.
DR TreeFam; TF314029; -.
DR PathwayCommons; P47224; -.
DR SignaLink; P47224; -.
DR BioGRID-ORCS; 5877; 189 hits in 1080 CRISPR screens.
DR EvolutionaryTrace; P47224; -.
DR GeneWiki; RABIF; -.
DR GenomeRNAi; 5877; -.
DR Pharos; P47224; Tbio.
DR PRO; PR:P47224; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P47224; protein.
DR Bgee; ENSG00000183155; Expressed in cervix squamous epithelium and 189 other tissues.
DR Genevisible; P47224; HS.
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; IDA:UniProtKB.
DR GO; GO:0061025; P:membrane fusion; TAS:ProtInc.
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_0000174174"
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:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CONFLICT 5..6
FT /note="EQ -> DE (in Ref. 1; AAB34955)"
FT /evidence="ECO:0000305"
FT STRAND 15..22
FT /evidence="ECO:0007829|PDB:2FU5"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:2FU5"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:2FU5"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:2FU5"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:2FU5"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:2FU5"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:2FU5"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:2FU5"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:2FU5"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:2FU5"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:2FU5"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:2FU5"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:2FU5"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:2FU5"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:2FU5"
SQ SEQUENCE 123 AA; 13839 MW; 78E98395FAE10257 CRC64;
MEPAEQPSEL VSAEGRNRKA VLCQRCGSRV LQPGTALFSR RQLFLPSMRK KPALSDGSNP
DGDLLQEHWL VEDMFIFENV GFTKDVGNIK FLVCADCEIG PIGWHCLDDK NSFYVALERV
SHE
