RPH3L_MOUSE
ID RPH3L_MOUSE Reviewed; 302 AA.
AC Q768S4; Q9D353;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Rab effector Noc2;
DE AltName: Full=No C2 domains protein;
DE AltName: Full=Rabphilin-3A-like protein;
GN Name=Rph3al; Synonyms=Gm1753, Noc2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, SUBCELLULAR
RP LOCATION, DOMAIN, AND MUTAGENESIS OF 51-GLU--ILE-55.
RC TISSUE=Brain;
RX PubMed=14722103; DOI=10.1074/jbc.m306812200;
RA Fukuda M., Kanno E., Yamamoto A.;
RT "Rabphilin and Noc2 are recruited to dense-core vesicles through specific
RT interaction with Rab27A in PC12 cells.";
RL J. Biol. Chem. 279:13065-13075(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND INTERACTION WITH
RP RAB3A; RAB3B; RAB3C AND RAB3D.
RX PubMed=15159548; DOI=10.1073/pnas.0306709101;
RA Matsumoto M., Miki T., Shibasaki T., Kawaguchi M., Shinozaki H., Nio J.,
RA Saraya A., Koseki H., Miyazaki M., Iwanaga T., Seino S.;
RT "Noc2 is essential in normal regulation of exocytosis in endocrine and
RT exocrine cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:8313-8318(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 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 [6]
RP CHARACTERIZATION, AND INTERACTION WITH RAB3A; RAB3B; RAB3C; RAB3D AND
RP RAB27A.
RX PubMed=12578829; DOI=10.1074/jbc.m212341200;
RA Fukuda M.;
RT "Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2.
RT Identification of a critical determinant of Rab3A/Rab27A recognition by
RT Rim2.";
RL J. Biol. Chem. 278:15373-15380(2003).
RN [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16835753; DOI=10.1007/s00418-006-0207-0;
RA Teramae H., Fujimoto W., Seino S., Iwanaga T.;
RT "Cellular expression of Noc2, a Rab effector protein, in endocrine and
RT exocrine tissues in the mouse.";
RL Histochem. Cell Biol. 127:1-11(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Rab GTPase effector involved in the late steps of regulated
CC exocytosis, both in endocrine and exocrine cells. Regulates the
CC exocytosis of dense-core vesicles in neuroendocrine cells through
CC interaction with RAB27A. Acts as a potential RAB3B effector protein in
CC epithelial cells. {ECO:0000269|PubMed:14722103,
CC ECO:0000269|PubMed:15159548}.
CC -!- SUBUNIT: Recruited to dense-core vesicles through specific interaction
CC with RAB27A in endocrine cells. Interacts with RAB3A, RAB3B, RAB3C and
CC RAB3D. Interacts with ZYX (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasmic vesicle, secretory vesicle
CC membrane. Note=Recruited to the exocytic secretory vesicles by RAB27A.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q768S4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q768S4-2; Sequence=VSP_023245, VSP_023246;
CC -!- TISSUE SPECIFICITY: Highly expressed in pancreatic islets. High to
CC moderate expression in adrenal gland, pituitary gland and ovary.
CC {ECO:0000269|PubMed:16835753}.
CC -!- DOMAIN: The N-terminus of the RabBD domain is necessary and sufficient
CC for interaction with RAB27A. {ECO:0000269|PubMed:14722103}.
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DR EMBL; AB112925; BAD07030.1; -; mRNA.
DR EMBL; AB158403; BAD18853.1; -; mRNA.
DR EMBL; AK018335; BAB31169.1; -; mRNA.
DR EMBL; AL731710; CAI24681.1; -; Genomic_DNA.
DR EMBL; AL731710; CAI24682.1; -; Genomic_DNA.
DR EMBL; AL669897; CAI24682.1; JOINED; Genomic_DNA.
DR EMBL; BC127960; AAI27961.1; -; mRNA.
DR CCDS; CCDS25058.1; -. [Q768S4-1]
DR CCDS; CCDS70243.1; -. [Q768S4-2]
DR RefSeq; NP_001278088.1; NM_001291159.1. [Q768S4-2]
DR RefSeq; NP_083824.1; NM_029548.4. [Q768S4-1]
DR RefSeq; XP_006533700.1; XM_006533637.1. [Q768S4-1]
DR RefSeq; XP_006533701.1; XM_006533638.3. [Q768S4-1]
DR RefSeq; XP_006533702.1; XM_006533639.3. [Q768S4-1]
DR RefSeq; XP_006533703.1; XM_006533640.3. [Q768S4-1]
DR RefSeq; XP_006533704.1; XM_006533641.3. [Q768S4-1]
DR RefSeq; XP_006533705.1; XM_006533642.3. [Q768S4-1]
DR RefSeq; XP_011247403.1; XM_011249101.1. [Q768S4-2]
DR RefSeq; XP_011247404.1; XM_011249102.1. [Q768S4-2]
DR AlphaFoldDB; Q768S4; -.
DR SMR; Q768S4; -.
DR BioGRID; 237613; 10.
DR IntAct; Q768S4; 1.
DR STRING; 10090.ENSMUSP00000113869; -.
DR iPTMnet; Q768S4; -.
DR PhosphoSitePlus; Q768S4; -.
DR MaxQB; Q768S4; -.
DR PaxDb; Q768S4; -.
DR PRIDE; Q768S4; -.
DR ProteomicsDB; 300442; -. [Q768S4-1]
DR ProteomicsDB; 300443; -. [Q768S4-2]
DR Antibodypedia; 10243; 223 antibodies from 27 providers.
DR DNASU; 380714; -.
DR Ensembl; ENSMUST00000021208; ENSMUSP00000021208; ENSMUSG00000020847. [Q768S4-2]
DR Ensembl; ENSMUST00000066504; ENSMUSP00000064202; ENSMUSG00000020847. [Q768S4-1]
DR Ensembl; ENSMUST00000108420; ENSMUSP00000104058; ENSMUSG00000020847. [Q768S4-2]
DR Ensembl; ENSMUST00000121287; ENSMUSP00000113869; ENSMUSG00000020847. [Q768S4-1]
DR GeneID; 380714; -.
DR KEGG; mmu:380714; -.
DR UCSC; uc007kew.2; mouse. [Q768S4-1]
DR UCSC; uc007kex.2; mouse. [Q768S4-2]
DR CTD; 9501; -.
DR MGI; MGI:1923492; Rph3al.
DR VEuPathDB; HostDB:ENSMUSG00000020847; -.
DR eggNOG; KOG1013; Eukaryota.
DR GeneTree; ENSGT00440000034248; -.
DR HOGENOM; CLU_076502_1_0_1; -.
DR InParanoid; Q768S4; -.
DR OMA; DCRKVRP; -.
DR OrthoDB; 374694at2759; -.
DR PhylomeDB; Q768S4; -.
DR TreeFam; TF342971; -.
DR BioGRID-ORCS; 380714; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Rph3al; mouse.
DR PRO; PR:Q768S4; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q768S4; protein.
DR Bgee; ENSMUSG00000020847; Expressed in primary oocyte and 153 other tissues.
DR ExpressionAtlas; Q768S4; baseline and differential.
DR Genevisible; Q768S4; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030141; C:secretory granule; ISO:MGI.
DR GO; GO:0030667; C:secretory granule membrane; ISO:MGI.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030274; F:LIM domain binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:MGI.
DR GO; GO:0042593; P:glucose homeostasis; IDA:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0045744; P:negative regulation of G protein-coupled receptor signaling pathway; IMP:MGI.
DR GO; GO:0032024; P:positive regulation of insulin secretion; IDA:UniProtKB.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISO:MGI.
DR GO; GO:0017158; P:regulation of calcium ion-dependent exocytosis; IMP:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0061669; P:spontaneous neurotransmitter secretion; IBA:GO_Central.
DR CDD; cd15763; FYVE_RPH3L; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR041282; FYVE_2.
DR InterPro; IPR041857; Noc2_FYVE.
DR InterPro; IPR010911; Rab_BD.
DR InterPro; IPR030538; Rab_effect_Noc2.
DR InterPro; IPR043566; Rabphilin/DOC2/Noc2.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45729; PTHR45729; 1.
DR PANTHER; PTHR45729:SF4; PTHR45729:SF4; 1.
DR Pfam; PF02318; FYVE_2; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50916; RABBD; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoplasmic vesicle; Exocytosis; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..302
FT /note="Rab effector Noc2"
FT /id="PRO_0000278264"
FT DOMAIN 41..158
FT /note="RabBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00234"
FT ZN_FING 89..146
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 174..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 118..141
FT /note="KVCTKCGIEASPGQKRPLWLCKIC -> LGIRWLQHFLESLLILNRDLTCSL
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023245"
FT VAR_SEQ 142..302
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023246"
FT MUTAGEN 51..55
FT /note="ELEII->ALEIA: Loss of binding to RAB27A, remaining
FT cytoplasmic."
FT /evidence="ECO:0000269|PubMed:14722103"
SQ SEQUENCE 302 AA; 33259 MW; 5AE4A68535653324 CRC64;
MADTIFSSGN DQWVCPNDRQ LALRAKLQTG WSVHTYQTEK QRRSQCLSPG ELEIILQVIQ
RAERLDILEQ QRIGRLVERL ETMQRNVMGN GLSQCLLCGE VLGFLGSSSV FCKDCRKKVC
TKCGIEASPG QKRPLWLCKI CSEQREVWKR SGAWFYKGLP KYILPLKTPG RADDPHFRPL
PVEPTETQPP SAETSRVYTW ARGRVVSSDS DSDSDLSSSS LEDRPLPSGV KGTKGDKPRG
DSGASMESPR LGPARPPSHL SGSQSSLGSE AGTGATEPQG GTPAQPEPRV PGKRHTWATP
RY
