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   27-MAR-2024, entry version 129.
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       Together with RAB11A and FIP3/RAB11FIP3, parts of the ciliary targeting
CC       complex that promotes preciliary vesicle trafficking to mother
CC       centriole and ciliogenesis initiation. Part of the ciliary targeting
CC       complex containing Rab11, ASAP1, RAB3IP and RAB11FIP3 and ARF4 that
CC       promotes RAB3IP preciliary vesicle trafficking to mother centriole and
CC       ciliogenesis initiation (By similarity). {ECO:0000250|UniProtKB:Q96QF0,
CC       ECO:0000269|PubMed:12221131}.
CC   -!- SUBUNIT: Homodimer (By similarity). Interacts with the N-terminal
CC       region of SSX2 (By similarity). Interacts with the GDP-bound forms of
CC       RAB8A and RAB8B (By similarity). The interaction with RAB8A is
CC       prevented by phosphorylation of RAB8A at 'Thr-72' (By similarity).
CC       Interacts with the GDP-bound forms of RAB3A and RAB3D (PubMed:7532276).
CC       Interacts with DCDC1 (By similarity) (PubMed:7532276). Interacts (via
CC       the N-terminal region) with TRAPPC14; this interaction mediates RAB3IP
CC       association with the TRAPP II complex (By similarity). Forms a
CC       heterotetramer with RAB11A where RAB3IP homodimer binds two RAB11A
CC       subunits. Forms a complex with RAB11A and RAB11FIP3, probably a
CC       heterohexamer with two of each protein subunit, where Rabin8/RAB3IP and
CC       RAB11FIP3 simultaneously bind to RAB11A; the complex promotes
CC       preciliary trafficking. Forms a complex containing RAB11A, ASAP1,
CC       RAB3IP, RAP11FIP3 and ARF4; the complex promotes preciliary
CC       trafficking; the complex binds to RHO in photoreceptor cells and
CC       promotes RHO ciliary transport (By similarity).
CC       {ECO:0000250|UniProtKB:Q96QF0, 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}.
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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   PhosphoSitePlus; Q62739; -.
DR   jPOST; Q62739; -.
DR   PaxDb; 10116-ENSRNOP00000007258; -.
DR   Ensembl; ENSRNOT00000007258.6; ENSRNOP00000007258.4; ENSRNOG00000005362.7.
DR   Ensembl; ENSRNOT00055022084; ENSRNOP00055017926; ENSRNOG00055012895.
DR   Ensembl; ENSRNOT00060014115; ENSRNOP00060010814; ENSRNOG00060008450.
DR   Ensembl; ENSRNOT00065021125; ENSRNOP00065016293; ENSRNOG00065012906.
DR   GeneID; 29885; -.
DR   KEGG; rno:29885; -.
DR   UCSC; RGD:620650; rat.
DR   AGR; RGD:620650; -.
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; WEIMQLR; -.
DR   OrthoDB; 1361004at2759; -.
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 cell types or 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:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
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   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   CDD; cd21068; Rab11BD_RAB3IP; 1.
DR   Gene3D; 1.20.5.4880; -; 1.
DR   InterPro; IPR040351; RAB3IL/RAB3IP/Sec2.
DR   InterPro; IPR009449; Sec2_N.
DR   PANTHER; PTHR14430:SF2; RAB-3A-INTERACTING PROTEIN; 1.
DR   PANTHER; PTHR14430; RABIN3-RELATED; 1.
DR   Pfam; PF06428; Sec2p; 1.
DR   SUPFAM; SSF144284; Sec2 N-terminal region; 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         149
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
//