RPH3L_HUMAN
ID RPH3L_HUMAN Reviewed; 315 AA.
AC Q9UNE2; D3DTG7; Q9BSB3;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 158.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=10395805; DOI=10.1006/geno.1999.5864;
RA Smith J.S., Tachibana I., Allen C., Chiappa S.A., Lee H.K., McIver B.,
RA Jenkins R.B., Raffel C.;
RT "Cloning of a human ortholog (RPH3AL) of (RNO)Rph3al from a candidate
RT 17p13.3 medulloblastoma tumor suppressor locus.";
RL Genomics 59:97-101(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Muscle;
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]
RP FUNCTION AS A RAB3B EFFECTOR, INTERACTION WITH RAB3B, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=15003533; DOI=10.1016/j.bbrc.2004.02.026;
RA Manabe S., Nishimura N., Yamamoto Y., Kitamura H., Morimoto S., Imai M.,
RA Nagahiro S., Seino S., Sasaki T.;
RT "Identification and characterization of Noc2 as a potential Rab3B effector
RT protein in epithelial cells.";
RL Biochem. Biophys. Res. Commun. 316:218-225(2004).
CC -!- FUNCTION: Rab GTPase effector involved in the late steps of regulated
CC exocytosis, both in endocrine and exocrine cells (By similarity). Acts
CC as a potential RAB3B effector protein in epithelial cells.
CC {ECO:0000250, ECO:0000269|PubMed:15003533}.
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 -!- INTERACTION:
CC Q9UNE2; X5D778: ANKRD11; NbExp=3; IntAct=EBI-2855824, EBI-17183751;
CC Q9UNE2; Q8N5M1: ATPAF2; NbExp=3; IntAct=EBI-2855824, EBI-1166928;
CC Q9UNE2; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-2855824, EBI-8643161;
CC Q9UNE2; A0A024R8L2: hCG_1987119; NbExp=3; IntAct=EBI-2855824, EBI-14103818;
CC Q9UNE2; P61978-2: HNRNPK; NbExp=3; IntAct=EBI-2855824, EBI-7060731;
CC Q9UNE2; O75525: KHDRBS3; NbExp=3; IntAct=EBI-2855824, EBI-722504;
CC Q9UNE2; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-2855824, EBI-10172526;
CC Q9UNE2; Q9UL41: PNMA3; NbExp=3; IntAct=EBI-2855824, EBI-11278955;
CC Q9UNE2; O43741: PRKAB2; NbExp=3; IntAct=EBI-2855824, EBI-1053424;
CC Q9UNE2; P61289: PSME3; NbExp=3; IntAct=EBI-2855824, EBI-355546;
CC Q9UNE2; O00194: RAB27B; NbExp=3; IntAct=EBI-2855824, EBI-10179046;
CC Q9UNE2; Q9UHP6: RSPH14; NbExp=3; IntAct=EBI-2855824, EBI-748350;
CC Q9UNE2; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-2855824, EBI-748391;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15003533}.
CC Cytoplasmic vesicle, secretory vesicle membrane
CC {ECO:0000269|PubMed:15003533}. Note=Recruited to the vesicle membrane
CC in a GTP- and RAB3B-dependent manner in epithelial cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UNE2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UNE2-2; Sequence=VSP_023244;
CC -!- TISSUE SPECIFICITY: Moderate to high levels of expression in thyroid,
CC ovary, stomach, heart, pancreas, skeletal muscle, kidney and liver.
CC Also detected in epithelial cells. {ECO:0000269|PubMed:10395805,
CC ECO:0000269|PubMed:15003533}.
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; AF129812; AAD45582.1; -; mRNA.
DR EMBL; AK000469; BAA91186.1; -; mRNA.
DR EMBL; CH471108; EAW90670.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90671.1; -; Genomic_DNA.
DR EMBL; BC005153; AAH05153.1; -; mRNA.
DR EMBL; BC093776; AAH93776.1; -; mRNA.
DR EMBL; BC113413; AAI13414.1; -; mRNA.
DR CCDS; CCDS10994.1; -. [Q9UNE2-1]
DR CCDS; CCDS54059.1; -. [Q9UNE2-2]
DR RefSeq; NP_001177340.1; NM_001190411.1. [Q9UNE2-1]
DR RefSeq; NP_001177341.1; NM_001190412.1. [Q9UNE2-2]
DR RefSeq; NP_001177342.1; NM_001190413.1. [Q9UNE2-2]
DR RefSeq; NP_008918.1; NM_006987.3. [Q9UNE2-1]
DR RefSeq; XP_011533669.1; XM_011535367.2.
DR RefSeq; XP_011533670.1; XM_011535368.2.
DR AlphaFoldDB; Q9UNE2; -.
DR SMR; Q9UNE2; -.
DR BioGRID; 114880; 22.
DR IntAct; Q9UNE2; 16.
DR STRING; 9606.ENSP00000328977; -.
DR iPTMnet; Q9UNE2; -.
DR PhosphoSitePlus; Q9UNE2; -.
DR BioMuta; RPH3AL; -.
DR DMDM; 74735140; -.
DR MassIVE; Q9UNE2; -.
DR PaxDb; Q9UNE2; -.
DR PeptideAtlas; Q9UNE2; -.
DR PRIDE; Q9UNE2; -.
DR ProteomicsDB; 85280; -. [Q9UNE2-1]
DR ProteomicsDB; 85281; -. [Q9UNE2-2]
DR Antibodypedia; 10243; 223 antibodies from 27 providers.
DR DNASU; 9501; -.
DR Ensembl; ENST00000323434.12; ENSP00000319210.8; ENSG00000181031.16. [Q9UNE2-2]
DR Ensembl; ENST00000331302.12; ENSP00000328977.7; ENSG00000181031.16. [Q9UNE2-1]
DR Ensembl; ENST00000536489.6; ENSP00000438224.2; ENSG00000181031.16. [Q9UNE2-2]
DR Ensembl; ENST00000608278.2; ENSP00000483035.1; ENSG00000262334.6. [Q9UNE2-1]
DR Ensembl; ENST00000608519.5; ENSP00000476394.1; ENSG00000262334.6. [Q9UNE2-2]
DR Ensembl; ENST00000618002.4; ENSP00000479485.1; ENSG00000181031.16. [Q9UNE2-1]
DR Ensembl; ENST00000632000.1; ENSP00000487689.1; ENSG00000262334.6. [Q9UNE2-2]
DR Ensembl; ENST00000632545.1; ENSP00000487851.1; ENSG00000262334.6. [Q9UNE2-2]
DR Ensembl; ENST00000632616.1; ENSP00000487649.1; ENSG00000262334.6. [Q9UNE2-1]
DR GeneID; 9501; -.
DR KEGG; hsa:9501; -.
DR MANE-Select; ENST00000331302.12; ENSP00000328977.7; NM_006987.4; NP_008918.1.
DR UCSC; uc002fre.3; human. [Q9UNE2-1]
DR CTD; 9501; -.
DR DisGeNET; 9501; -.
DR GeneCards; RPH3AL; -.
DR HGNC; HGNC:10296; RPH3AL.
DR HPA; ENSG00000181031; Tissue enhanced (pancreas, pituitary gland).
DR MIM; 604881; gene.
DR neXtProt; NX_Q9UNE2; -.
DR OpenTargets; ENSG00000181031; -.
DR PharmGKB; PA34658; -.
DR VEuPathDB; HostDB:ENSG00000181031; -.
DR eggNOG; KOG1013; Eukaryota.
DR GeneTree; ENSGT00440000034248; -.
DR HOGENOM; CLU_076502_1_0_1; -.
DR InParanoid; Q9UNE2; -.
DR OMA; DCRKVRP; -.
DR OrthoDB; 542090at2759; -.
DR PhylomeDB; Q9UNE2; -.
DR TreeFam; TF342971; -.
DR PathwayCommons; Q9UNE2; -.
DR SignaLink; Q9UNE2; -.
DR BioGRID-ORCS; 9501; 11 hits in 1069 CRISPR screens.
DR ChiTaRS; RPH3AL; human.
DR GeneWiki; RPH3AL; -.
DR GenomeRNAi; 9501; -.
DR Pharos; Q9UNE2; Tbio.
DR PRO; PR:Q9UNE2; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9UNE2; protein.
DR Bgee; ENSG00000181031; Expressed in body of pancreas and 94 other tissues.
DR ExpressionAtlas; Q9UNE2; baseline and differential.
DR Genevisible; Q9UNE2; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008092; F:cytoskeletal protein binding; TAS:ProtInc.
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; IEA:Ensembl.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0045744; P:negative regulation of G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0032024; P:positive regulation of insulin secretion; IEA:Ensembl.
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 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoplasmic vesicle; Exocytosis; Membrane;
KW Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..315
FT /note="Rab effector Noc2"
FT /id="PRO_0000278263"
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 170..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..273
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 VAR_SEQ 118..146
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023244"
FT CONFLICT 85
FT /note="R -> Q (in Ref. 4; AAH05153)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 315 AA; 34464 MW; FDDB315E0BBC7C23 CRC64;
MADTIFGSGN DQWVCPNDRQ LALRAKLQTG WSVHTYQTEK QRRKQHLSPA EVEAILQVIQ
RAERLDVLEQ QRIGRLVERL ETMRRNVMGN GLSQCLLCGE VLGFLGSSSV FCKDCRKKVC
TKCGIEASPG QKRPLWLCKI CSEQREVWKR SGAWFYKGLP KYILPLKTPG RADDPHFRPL
PTEPAEREPR SSETSRIYTW ARGRVVSSDS DSDSDLSSSS LEDRLPSTGV RDRKGDKPWK
ESGGSVEAPR MGFTHPPGHL SGCQSSLASG ETGTGSADPP GGPRPGLTRR APVKDTPGRA
PAADAAPAGP SSCLG
