RPH3L_BOVIN
ID RPH3L_BOVIN Reviewed; 292 AA.
AC Q58D79;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Rab GTPase effector involved in the late steps of regulated
CC exocytosis, both in endocrine and exocrine cells. {ECO:0000250}.
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 {ECO:0000250}. Cytoplasmic vesicle,
CC secretory vesicle membrane {ECO:0000250}.
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; BT021718; AAX46565.1; -; mRNA.
DR EMBL; BC102095; AAI02096.1; -; mRNA.
DR RefSeq; NP_001030571.1; NM_001035494.1.
DR AlphaFoldDB; Q58D79; -.
DR SMR; Q58D79; -.
DR STRING; 9913.ENSBTAP00000050227; -.
DR PaxDb; Q58D79; -.
DR PRIDE; Q58D79; -.
DR GeneID; 617294; -.
DR KEGG; bta:617294; -.
DR CTD; 9501; -.
DR eggNOG; KOG1013; Eukaryota.
DR HOGENOM; CLU_076502_1_0_1; -.
DR InParanoid; Q58D79; -.
DR OrthoDB; 374694at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
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:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0017158; P:regulation of calcium ion-dependent exocytosis; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Cytoplasm; Cytoplasmic vesicle; Exocytosis; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..292
FT /note="Rab effector Noc2"
FT /id="PRO_0000278262"
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 175..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..278
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 292 AA; 32043 MW; BC475BD9D5503438 CRC64;
MADTIFGSGC DQWVCPNDRQ LALRAKLHTG WSVHTYQTEK QRKSQSLSPA EVEAILQVIQ
RAERLDILEQ QRVGRLVERL ETMRRNVMGN GLSQCLLCGE VLGFLGSSSV FCKDCRKKVC
TKCGIEASPS QKRPLWLCKI CSEQREVWKR SGAWFYKGIP KFILPLKIPG QADHPSFRPL
PVEPAEQEPR STETSRVYTW ARGRVVSSDS DSDSDLSSSS LDDRLRPAGV RDPKGNKPWG
ESGGSVESLK MGPTRPASCL SGSQSSLASE TGTGSADPQG GPRTLAGPRG PR
