RAB3I_RAT
ID RAB3I_RAT Reviewed; 460 AA.
AC Q62739; A1L127;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Rab-3A-interacting protein;
DE Short=Rab3A-interacting protein;
DE AltName: Full=Rabin-3;
DE AltName: Full=SSX2-interacting protein;
GN Name=Rab3ip; Synonyms=Rabin3, Rabin8;
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], INTERACTION WITH RAB3A AND RAB3D, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Fischer 344 {ECO:0000312|EMBL:AAA67890.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAA67890.1};
RX PubMed=7532276; DOI=10.1128/mcb.15.3.1137;
RA Brondyk W.H., McKiernan C.J., Fortner K.A., Stabila P., Holz R.W.,
RA Macara I.G.;
RT "Interaction cloning of Rabin3, a novel protein that associates with the
RT Ras-like GTPase Rab3A.";
RL Mol. Cell. Biol. 15:1137-1143(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis {ECO:0000312|EMBL:AAI27501.1};
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 [5] {ECO:0007744|PubMed:22673903}
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).
RN [6]
RP FUNCTION.
RX PubMed=12221131; DOI=10.1091/mbc.e02-03-0143;
RA Hattula K., Furuhjelm J., Arffman A., Peranen J.;
RT "A Rab8-specific GDP/GTP exchange factor is involved in actin remodeling
RT and polarized membrane transport.";
RL Mol. Biol. Cell 13:3268-3280(2002).
CC -!- FUNCTION: Guanine nucleotide exchange factor (GEF) which may activate
CC RAB8A and RAB8B (PubMed:12221131). Promotes the exchange of GDP to GTP,
CC converting inactive GDP-bound Rab proteins into their active GTP-bound
CC form (PubMed:12221131). Mediates the release of GDP from RAB8A and
CC RAB8B but not from RAB3A or RAB5 (By similarity). Modulates actin
CC organization and promotes polarized transport of RAB8A-specific
CC vesicles to the cell surface (PubMed:12221131). Together with RAB11A,
CC RAB8A, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP
CC promotes transcytosis of PODXL to the apical membrane initiation sites
CC (AMIS), apical surface formation and lumenogenesis (By similarity).
CC {ECO:0000250|UniProtKB:Q96QF0, ECO:0000269|PubMed:12221131}.
CC -!- SUBUNIT: Interacts with the N-terminal region of SSX2 (By similarity).
CC Interacts with the GDP-bound forms of RAB8A and RAB8B (By similarity).
CC The interaction with RAB8A is prevented by phosphorylation of RAB8A at
CC 'Thr-72' (By similarity). Interacts with the GDP-bound forms of RAB3A
CC and RAB3D (PubMed:7532276). Interacts with DCDC1 (By similarity)
CC (PubMed:7532276). Interacts (via the N-terminal region) with TRAPPC14;
CC this interaction mediates RAB3IP association with the TRAPP II complex
CC (By similarity). {ECO:0000250|UniProtKB:Q96QF0,
CC ECO:0000269|PubMed:7532276}.
CC -!- INTERACTION:
CC Q62739; Q8R313: Exoc6; Xeno; NbExp=2; IntAct=EBI-2028671, EBI-9202179;
CC Q62739; P62492: Rab11a; Xeno; NbExp=4; IntAct=EBI-2028671, EBI-770256;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7532276}. Nucleus
CC {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection,
CC lamellipodium {ECO:0000250}. Note=Predominantly cytoplasmic but a small
CC proportion colocalizes with SSX2 in the nucleus. Activation of protein
CC kinase C results in redistribution to the periphery of lamellipodia. In
CC the cytoskeleton, localizes to cortical actin (By similarity).
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed at highest level
CC in testis. {ECO:0000269|PubMed:7532276}.
CC -!- SIMILARITY: Belongs to the SEC2 family. {ECO:0000255}.
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; U19181; AAA67890.1; -; mRNA.
DR EMBL; AABR07057194; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC127500; AAI27501.1; -; mRNA.
DR EMBL; CH473960; EDM16646.1; -; Genomic_DNA.
DR EMBL; CH473960; EDM16647.1; -; Genomic_DNA.
DR PIR; I57546; I57546.
DR RefSeq; NP_059009.2; NM_017313.3.
DR RefSeq; XP_006241419.1; XM_006241357.3.
DR RefSeq; XP_006241420.1; XM_006241358.2.
DR RefSeq; XP_006241421.1; XM_006241359.3.
DR RefSeq; XP_006241422.1; XM_006241360.3.
DR AlphaFoldDB; Q62739; -.
DR SMR; Q62739; -.
DR IntAct; Q62739; 4.
DR MINT; Q62739; -.
DR STRING; 10116.ENSRNOP00000007258; -.
DR jPOST; Q62739; -.
DR PaxDb; Q62739; -.
DR PRIDE; Q62739; -.
DR Ensembl; ENSRNOT00000007258; ENSRNOP00000007258; ENSRNOG00000005362.
DR GeneID; 29885; -.
DR KEGG; rno:29885; -.
DR UCSC; RGD:620650; rat.
DR CTD; 117177; -.
DR RGD; 620650; Rab3ip.
DR eggNOG; KOG4324; Eukaryota.
DR GeneTree; ENSGT00940000157998; -.
DR HOGENOM; CLU_038204_2_0_1; -.
DR InParanoid; Q62739; -.
DR OMA; WAMASEP; -.
DR OrthoDB; 619794at2759; -.
DR PhylomeDB; Q62739; -.
DR TreeFam; TF313748; -.
DR Reactome; R-RNO-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-RNO-5620916; VxPx cargo-targeting to cilium.
DR Reactome; R-RNO-5620922; BBSome-mediated cargo-targeting to cilium.
DR Reactome; R-RNO-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR PRO; PR:Q62739; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Proteomes; UP000234681; Chromosome 7.
DR Bgee; ENSRNOG00000005362; Expressed in kidney and 20 other tissues.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070319; C:Golgi to plasma membrane transport vesicle; IBA:GO_Central.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:1990635; C:proximal dendrite; IDA:RGD.
DR GO; GO:0051020; F:GTPase binding; IPI:RGD.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:RGD.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0051490; P:negative regulation of filopodium assembly; IMP:RGD.
DR GO; GO:0006612; P:protein targeting to membrane; ISO:RGD.
DR InterPro; IPR040351; RAB3IL/RAB3IP/Sec2.
DR InterPro; IPR009449; Sec2_N.
DR PANTHER; PTHR14430; PTHR14430; 1.
DR Pfam; PF06428; Sec2p; 1.
PE 1: Evidence at protein level;
KW Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW Guanine-nucleotide releasing factor; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..460
FT /note="Rab-3A-interacting protein"
FT /id="PRO_0000097146"
FT REGION 246..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 149..244
FT /evidence="ECO:0000255"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QF0"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68EF0"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QF0"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QF0"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68EF0"
FT CONFLICT 258
FT /note="A -> D (in Ref. 1; AAA67890)"
FT CONFLICT 265
FT /note="R -> G (in Ref. 1; AAA67890)"
FT CONFLICT 289
FT /note="P -> A (in Ref. 1; AAA67890)"
SQ SEQUENCE 460 AA; 51032 MW; 6DFAA787292E7577 CRC64;
MANDPLEGFH EVNLASPTSP DLLGVCDPGT QEQTTSPSVI YRPHPSTLCS ATIQANALNL
SDLPTQPVYS SPRHLNCAEI SNISIHVPEP ASSVASEVAA GLTRFTSRKD SCNAEREFLQ
GATVTEASAG NDDIFGLSTD SLSRLRSPSV LEVREKGYER LKEELAKAQR ELKLKDEECE
RLSKVRDQLG QELEELTASL FEEAHKMVRE ANVKQATAEK QLKEAQGKID VLQAEVAALK
TLVLSSSPTS PTQEPLAAGK TPFKRGHTRN KSTSSAMSGS HQDFSAIQPI VKDCREADLS
LYNEFRSWKD EPTMDRTCPF LDKIYQEDIF PCLTFAKSEL ASAVLEAVEN NTLSIEPVGL
QPIRFVKASA VECGGPKKCA LTGQSKPCKH RIKLGDSSSY YYISPVCRYR ITSVCNFFTY
IRYIQQGLVK QQDVDQMFWE VMQLRKEMSL AKLGYFKEEL
