RPH3L_RAT
ID RPH3L_RAT Reviewed; 302 AA.
AC O54880;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Rab effector Noc2;
DE AltName: Full=No C2 domains protein;
DE AltName: Full=Rabphilin-3A-like protein;
GN Name=Rph3al; Synonyms=Noc2;
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], FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INTERACTION WITH ZYX.
RC TISSUE=Insulinoma;
RX PubMed=9367993; DOI=10.1074/jbc.272.47.29407;
RA Kotake K., Ozaki N., Mizuta M., Sekiya S., Inagaki N., Seino S.;
RT "Noc2, a putative zinc finger protein involved in exocytosis in endocrine
RT cells.";
RL J. Biol. Chem. 272:29407-29410(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP FUNCTION, AND INTERACTION WITH RAB3A.
RX PubMed=11134008; DOI=10.1074/jbc.m006959200;
RA Haynes L.P., Evans G.J., Morgan A., Burgoyne R.D.;
RT "A direct inhibitory role for the Rab3-specific effector, Noc2, in Ca2+-
RT regulated exocytosis in neuroendocrine cells.";
RL J. Biol. Chem. 276:9726-9732(2001).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RAB27A.
RX PubMed=17067543; DOI=10.1016/j.abb.2006.09.021;
RA Imai A., Yoshie S., Nashida T., Shimomura H., Fukuda M.;
RT "Functional involvement of Noc2, a Rab27 effector, in rat parotid acinar
RT cells.";
RL Arch. Biochem. Biophys. 455:127-135(2006).
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:11134008,
CC ECO:0000269|PubMed:17067543, ECO:0000269|PubMed:9367993}.
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. {ECO:0000269|PubMed:11134008,
CC ECO:0000269|PubMed:17067543, ECO:0000269|PubMed:9367993}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasmic vesicle, secretory vesicle
CC membrane. Note=Recruited to the exocytic secretory vesicles by RAB27A.
CC -!- TISSUE SPECIFICITY: Highly expressed in pancreatic islets and parotid.
CC High to moderate expression in adrenal gland, pituitary gland and
CC ovary. {ECO:0000269|PubMed:9367993}.
CC -!- DOMAIN: The N-terminus of the RabBD domain is necessary and sufficient
CC for interaction with RAB27A. {ECO:0000250}.
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DR EMBL; AF022774; AAB95448.1; -; mRNA.
DR EMBL; BC091126; AAH91126.1; -; mRNA.
DR RefSeq; NP_598275.1; NM_133591.2.
DR RefSeq; XP_008766163.1; XM_008767941.2.
DR RefSeq; XP_008766164.1; XM_008767942.2.
DR AlphaFoldDB; O54880; -.
DR SMR; O54880; -.
DR BioGRID; 251130; 1.
DR STRING; 10116.ENSRNOP00000008697; -.
DR PaxDb; O54880; -.
DR PRIDE; O54880; -.
DR Ensembl; ENSRNOT00000081725; ENSRNOP00000075521; ENSRNOG00000061429.
DR GeneID; 171123; -.
DR KEGG; rno:171123; -.
DR CTD; 9501; -.
DR RGD; 620342; Rph3al.
DR eggNOG; KOG1013; Eukaryota.
DR GeneTree; ENSGT00440000034248; -.
DR HOGENOM; CLU_076502_1_0_1; -.
DR InParanoid; O54880; -.
DR OMA; DCRKVRP; -.
DR OrthoDB; 374694at2759; -.
DR PhylomeDB; O54880; -.
DR TreeFam; TF342971; -.
DR PRO; PR:O54880; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000061429; Expressed in ovary and 20 other tissues.
DR Genevisible; O54880; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0030141; C:secretory granule; IDA:RGD.
DR GO; GO:0030667; C:secretory granule membrane; IDA:RGD.
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; IPI:RGD.
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; IEA:Ensembl.
DR GO; GO:0042593; P:glucose homeostasis; ISO:RGD.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0045744; P:negative regulation of G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0032024; P:positive regulation of insulin secretion; ISO:RGD.
DR GO; GO:0050714; P:positive regulation of protein secretion; IMP:RGD.
DR GO; GO:0017158; P:regulation of calcium ion-dependent exocytosis; ISO:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
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 Cytoplasm; Cytoplasmic vesicle; Exocytosis; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..302
FT /note="Rab effector Noc2"
FT /id="PRO_0000278265"
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..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..276
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:0000250|UniProtKB:Q768S4"
SQ SEQUENCE 302 AA; 33433 MW; F7B24EE46CBC43F5 CRC64;
MADTIFSSGN DQWVCPNDRQ LALRAKLQTG WSVHTYQTEK QRRTQCLSPG EVEVILQVIQ
RAERLDILEQ QRIGRLVERL ETMQKNVMGN GVSQCLLCGE MLGFLGSSSV FCKDCRKKVC
TKCGIEASPG QKRPLWLCKI CSEQREVWKR SGAWFYKGLP KYILPLKTPG RADDPHFRPL
PVEPTEPQPQ SAEVSRVYTW ARGRVVSSDS DSDSDLSSSS LEDRPMPSGI KGTKYDKPRG
DSGGSMESPR MGPARPPSHL SGSQSSLGSE TGAGATDPQG GTLPRPEPRV SGKRHTWATT
HY
