Full text data of RPH3A
RPH3A
(KIAA0985)
[Confidence: low (only semi-automatic identification from reviews)]
Rabphilin-3A (Exophilin-1)
Rabphilin-3A (Exophilin-1)
UniProt
Q9Y2J0
ID RP3A_HUMAN Reviewed; 694 AA.
AC Q9Y2J0; B7Z3C3; Q96AE0;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 122.
DE RecName: Full=Rabphilin-3A;
DE AltName: Full=Exophilin-1;
GN Name=RPH3A; Synonyms=KIAA0985;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
RA Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hippocampus;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Protein transport. Probably involved with Ras-related
CC protein Rab-3A in synaptic vesicle traffic and/or synaptic vesicle
CC fusion. Could play a role in neurotransmitter release by
CC regulating membrane flow in the nerve terminal (By similarity).
CC -!- SUBUNIT: Monomer. Interacts with RAB3A, RAB3B, RAB3C, RAB3D,
CC RAB8A, RAB27A and RAB27B (By similarity).
CC -!- INTERACTION:
CC O14936:CASK; NbExp=3; IntAct=EBI-1216802, EBI-1215506;
CC -!- SUBCELLULAR LOCATION: Cell junction, synapse (By similarity).
CC Membrane; Peripheral membrane protein (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y2J0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y2J0-2; Sequence=VSP_021016;
CC -!- DOMAIN: Binds calcium via the C2 domains. The calcium-bound C2
CC domains mediate interactions with phospholipid bilayers (By
CC similarity).
CC -!- SIMILARITY: Contains 2 C2 domains.
CC -!- SIMILARITY: Contains 1 FYVE-type zinc finger.
CC -!- SIMILARITY: Contains 1 RabBD (Rab-binding) domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA76829.2; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB023202; BAA76829.2; ALT_INIT; mRNA.
DR EMBL; AK295696; BAH12159.1; -; mRNA.
DR EMBL; BC017259; AAH17259.1; -; mRNA.
DR RefSeq; NP_001137326.1; NM_001143854.1.
DR RefSeq; NP_055769.2; NM_014954.3.
DR RefSeq; XP_005253913.1; XM_005253856.1.
DR UniGene; Hs.21239; -.
DR ProteinModelPortal; Q9Y2J0; -.
DR SMR; Q9Y2J0; 48-170, 392-690.
DR IntAct; Q9Y2J0; 1.
DR MINT; MINT-199741; -.
DR STRING; 9606.ENSP00000413254; -.
DR PhosphoSite; Q9Y2J0; -.
DR DMDM; 13878745; -.
DR PaxDb; Q9Y2J0; -.
DR PRIDE; Q9Y2J0; -.
DR Ensembl; ENST00000389385; ENSP00000374036; ENSG00000089169.
DR Ensembl; ENST00000415485; ENSP00000405357; ENSG00000089169.
DR Ensembl; ENST00000420983; ENSP00000408889; ENSG00000089169.
DR Ensembl; ENST00000543106; ENSP00000440384; ENSG00000089169.
DR Ensembl; ENST00000551052; ENSP00000448297; ENSG00000089169.
DR GeneID; 22895; -.
DR KEGG; hsa:22895; -.
DR UCSC; uc001ttz.3; human.
DR CTD; 22895; -.
DR GeneCards; GC12P113012; -.
DR HGNC; HGNC:17056; RPH3A.
DR HPA; HPA002475; -.
DR MIM; 612159; gene.
DR neXtProt; NX_Q9Y2J0; -.
DR PharmGKB; PA134886118; -.
DR eggNOG; NOG247952; -.
DR HOGENOM; HOG000294226; -.
DR HOVERGEN; HBG017739; -.
DR InParanoid; Q9Y2J0; -.
DR OMA; SACVVCE; -.
DR OrthoDB; EOG7CZK67; -.
DR ChiTaRS; RPH3A; human.
DR GeneWiki; RPH3A; -.
DR GenomeRNAi; 22895; -.
DR NextBio; 43515; -.
DR PRO; PR:Q9Y2J0; -.
DR ArrayExpress; Q9Y2J0; -.
DR Bgee; Q9Y2J0; -.
DR CleanEx; HS_RPH3A; -.
DR Genevestigator; Q9Y2J0; -.
DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008021; C:synaptic vesicle; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; ISS:UniProtKB.
DR GO; GO:0005215; F:transporter activity; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR001565; Synaptotagmin.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR010911; Znf_FYVE-typ.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF02318; FYVE_2; 1.
DR PRINTS; PR00360; C2DOMAIN.
DR PRINTS; PR00399; SYNAPTOTAGMN.
DR SMART; SM00239; C2; 2.
DR SUPFAM; SSF49562; SSF49562; 2.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS50916; RABBD; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell junction; Complete proteome;
KW Lipid-binding; Membrane; Metal-binding; Protein transport;
KW Reference proteome; Repeat; Synapse; Transport; Zinc; Zinc-finger.
FT CHAIN 1 694 Rabphilin-3A.
FT /FTId=PRO_0000190227.
FT DOMAIN 44 160 RabBD.
FT DOMAIN 394 498 C2 1.
FT DOMAIN 552 655 C2 2.
FT ZN_FING 92 148 FYVE-type.
FT COMPBIAS 162 375 Pro-rich.
FT METAL 422 422 Calcium 1; via carbonyl oxygen (By
FT similarity).
FT METAL 423 423 Calcium 1 (By similarity).
FT METAL 423 423 Calcium 2 (By similarity).
FT METAL 429 429 Calcium 2 (By similarity).
FT METAL 484 484 Calcium 1 (By similarity).
FT METAL 484 484 Calcium 2 (By similarity).
FT METAL 485 485 Calcium 2; via carbonyl oxygen (By
FT similarity).
FT METAL 486 486 Calcium 1 (By similarity).
FT METAL 486 486 Calcium 2 (By similarity).
FT METAL 492 492 Calcium 1 (By similarity).
FT METAL 539 539 Calcium 3; via carbonyl oxygen (By
FT similarity).
FT METAL 581 581 Calcium 3 (By similarity).
FT METAL 581 581 Calcium 4 (By similarity).
FT METAL 587 587 Calcium 3 (By similarity).
FT METAL 641 641 Calcium 3 (By similarity).
FT METAL 641 641 Calcium 4 (By similarity).
FT METAL 642 642 Calcium 3; via carbonyl oxygen (By
FT similarity).
FT METAL 643 643 Calcium 3 (By similarity).
FT METAL 643 643 Calcium 4 (By similarity).
FT METAL 649 649 Calcium 4 (By similarity).
FT VAR_SEQ 24 28 NDKEQ -> K (in isoform 2).
FT /FTId=VSP_021016.
SQ SEQUENCE 694 AA; 76872 MW; BD9C43F306A04D69 CRC64;
MTDTVFSNSS NRWMYPSDRP LQSNDKEQLQ AGWSVHPGGQ PDRQRKQEEL TDEEKEIINR
VIARAEKMEE MEQERIGRLV DRLENMRKNV AGDGVNRCIL CGEQLGMLGS ACVVCEDCKK
NVCTKCGVET NNRLHSVWLC KICIEQREVW KRSGAWFFKG FPKQVLPQPM PIKKTKPQQP
VSEPAAPEQP APEPKHPARA PARGDSEDRR GPGQKTGPDP ASAPGRGNYG PPVRRASEAR
MSSSSRDSES WDHSGGAGDS SRSPAGLRRA NSVQASRPAP GSVQSPAPPQ PGQPGTPGGS
RPGPGPAGRF PDQKPEVAPS DPGTTAPPRE ERTGGVGGYP AVGAREDRMS HPSGPYSQAS
AAAPQPAAAR QPPPPEEEEE EANSYDSDEA TTLGALEFSL LYDQDNSSLQ CTIIKAKGLK
PMDSNGLADP YVKLHLLPGA SKSNKLRTKT LRNTRNPIWN ETLVYHGITD EDMQRKTLRI
SVCDEDKFGH NEFIGETRFS LKKLKPNQRK NFNICLERVI PMKRAGTTGS ARGMALYEEE
QVERVGDIEE RGKILVSLMY STQQGGLIVG IIRCVHLAAM DANGYSDPFV KLWLKPDMGK
KAKHKTQIKK KTLNPEFNEE FFYDIKHSDL AKKSLDISVW DYDIGKSNDY IGGCQLGISA
KGERLKHWYE CLKNKDKKIE RWHQLQNENH VSSD
//
ID RP3A_HUMAN Reviewed; 694 AA.
AC Q9Y2J0; B7Z3C3; Q96AE0;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 122.
DE RecName: Full=Rabphilin-3A;
DE AltName: Full=Exophilin-1;
GN Name=RPH3A; Synonyms=KIAA0985;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
RA Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hippocampus;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Protein transport. Probably involved with Ras-related
CC protein Rab-3A in synaptic vesicle traffic and/or synaptic vesicle
CC fusion. Could play a role in neurotransmitter release by
CC regulating membrane flow in the nerve terminal (By similarity).
CC -!- SUBUNIT: Monomer. Interacts with RAB3A, RAB3B, RAB3C, RAB3D,
CC RAB8A, RAB27A and RAB27B (By similarity).
CC -!- INTERACTION:
CC O14936:CASK; NbExp=3; IntAct=EBI-1216802, EBI-1215506;
CC -!- SUBCELLULAR LOCATION: Cell junction, synapse (By similarity).
CC Membrane; Peripheral membrane protein (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y2J0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y2J0-2; Sequence=VSP_021016;
CC -!- DOMAIN: Binds calcium via the C2 domains. The calcium-bound C2
CC domains mediate interactions with phospholipid bilayers (By
CC similarity).
CC -!- SIMILARITY: Contains 2 C2 domains.
CC -!- SIMILARITY: Contains 1 FYVE-type zinc finger.
CC -!- SIMILARITY: Contains 1 RabBD (Rab-binding) domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA76829.2; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB023202; BAA76829.2; ALT_INIT; mRNA.
DR EMBL; AK295696; BAH12159.1; -; mRNA.
DR EMBL; BC017259; AAH17259.1; -; mRNA.
DR RefSeq; NP_001137326.1; NM_001143854.1.
DR RefSeq; NP_055769.2; NM_014954.3.
DR RefSeq; XP_005253913.1; XM_005253856.1.
DR UniGene; Hs.21239; -.
DR ProteinModelPortal; Q9Y2J0; -.
DR SMR; Q9Y2J0; 48-170, 392-690.
DR IntAct; Q9Y2J0; 1.
DR MINT; MINT-199741; -.
DR STRING; 9606.ENSP00000413254; -.
DR PhosphoSite; Q9Y2J0; -.
DR DMDM; 13878745; -.
DR PaxDb; Q9Y2J0; -.
DR PRIDE; Q9Y2J0; -.
DR Ensembl; ENST00000389385; ENSP00000374036; ENSG00000089169.
DR Ensembl; ENST00000415485; ENSP00000405357; ENSG00000089169.
DR Ensembl; ENST00000420983; ENSP00000408889; ENSG00000089169.
DR Ensembl; ENST00000543106; ENSP00000440384; ENSG00000089169.
DR Ensembl; ENST00000551052; ENSP00000448297; ENSG00000089169.
DR GeneID; 22895; -.
DR KEGG; hsa:22895; -.
DR UCSC; uc001ttz.3; human.
DR CTD; 22895; -.
DR GeneCards; GC12P113012; -.
DR HGNC; HGNC:17056; RPH3A.
DR HPA; HPA002475; -.
DR MIM; 612159; gene.
DR neXtProt; NX_Q9Y2J0; -.
DR PharmGKB; PA134886118; -.
DR eggNOG; NOG247952; -.
DR HOGENOM; HOG000294226; -.
DR HOVERGEN; HBG017739; -.
DR InParanoid; Q9Y2J0; -.
DR OMA; SACVVCE; -.
DR OrthoDB; EOG7CZK67; -.
DR ChiTaRS; RPH3A; human.
DR GeneWiki; RPH3A; -.
DR GenomeRNAi; 22895; -.
DR NextBio; 43515; -.
DR PRO; PR:Q9Y2J0; -.
DR ArrayExpress; Q9Y2J0; -.
DR Bgee; Q9Y2J0; -.
DR CleanEx; HS_RPH3A; -.
DR Genevestigator; Q9Y2J0; -.
DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008021; C:synaptic vesicle; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; ISS:UniProtKB.
DR GO; GO:0005215; F:transporter activity; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR001565; Synaptotagmin.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR010911; Znf_FYVE-typ.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF02318; FYVE_2; 1.
DR PRINTS; PR00360; C2DOMAIN.
DR PRINTS; PR00399; SYNAPTOTAGMN.
DR SMART; SM00239; C2; 2.
DR SUPFAM; SSF49562; SSF49562; 2.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS50916; RABBD; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell junction; Complete proteome;
KW Lipid-binding; Membrane; Metal-binding; Protein transport;
KW Reference proteome; Repeat; Synapse; Transport; Zinc; Zinc-finger.
FT CHAIN 1 694 Rabphilin-3A.
FT /FTId=PRO_0000190227.
FT DOMAIN 44 160 RabBD.
FT DOMAIN 394 498 C2 1.
FT DOMAIN 552 655 C2 2.
FT ZN_FING 92 148 FYVE-type.
FT COMPBIAS 162 375 Pro-rich.
FT METAL 422 422 Calcium 1; via carbonyl oxygen (By
FT similarity).
FT METAL 423 423 Calcium 1 (By similarity).
FT METAL 423 423 Calcium 2 (By similarity).
FT METAL 429 429 Calcium 2 (By similarity).
FT METAL 484 484 Calcium 1 (By similarity).
FT METAL 484 484 Calcium 2 (By similarity).
FT METAL 485 485 Calcium 2; via carbonyl oxygen (By
FT similarity).
FT METAL 486 486 Calcium 1 (By similarity).
FT METAL 486 486 Calcium 2 (By similarity).
FT METAL 492 492 Calcium 1 (By similarity).
FT METAL 539 539 Calcium 3; via carbonyl oxygen (By
FT similarity).
FT METAL 581 581 Calcium 3 (By similarity).
FT METAL 581 581 Calcium 4 (By similarity).
FT METAL 587 587 Calcium 3 (By similarity).
FT METAL 641 641 Calcium 3 (By similarity).
FT METAL 641 641 Calcium 4 (By similarity).
FT METAL 642 642 Calcium 3; via carbonyl oxygen (By
FT similarity).
FT METAL 643 643 Calcium 3 (By similarity).
FT METAL 643 643 Calcium 4 (By similarity).
FT METAL 649 649 Calcium 4 (By similarity).
FT VAR_SEQ 24 28 NDKEQ -> K (in isoform 2).
FT /FTId=VSP_021016.
SQ SEQUENCE 694 AA; 76872 MW; BD9C43F306A04D69 CRC64;
MTDTVFSNSS NRWMYPSDRP LQSNDKEQLQ AGWSVHPGGQ PDRQRKQEEL TDEEKEIINR
VIARAEKMEE MEQERIGRLV DRLENMRKNV AGDGVNRCIL CGEQLGMLGS ACVVCEDCKK
NVCTKCGVET NNRLHSVWLC KICIEQREVW KRSGAWFFKG FPKQVLPQPM PIKKTKPQQP
VSEPAAPEQP APEPKHPARA PARGDSEDRR GPGQKTGPDP ASAPGRGNYG PPVRRASEAR
MSSSSRDSES WDHSGGAGDS SRSPAGLRRA NSVQASRPAP GSVQSPAPPQ PGQPGTPGGS
RPGPGPAGRF PDQKPEVAPS DPGTTAPPRE ERTGGVGGYP AVGAREDRMS HPSGPYSQAS
AAAPQPAAAR QPPPPEEEEE EANSYDSDEA TTLGALEFSL LYDQDNSSLQ CTIIKAKGLK
PMDSNGLADP YVKLHLLPGA SKSNKLRTKT LRNTRNPIWN ETLVYHGITD EDMQRKTLRI
SVCDEDKFGH NEFIGETRFS LKKLKPNQRK NFNICLERVI PMKRAGTTGS ARGMALYEEE
QVERVGDIEE RGKILVSLMY STQQGGLIVG IIRCVHLAAM DANGYSDPFV KLWLKPDMGK
KAKHKTQIKK KTLNPEFNEE FFYDIKHSDL AKKSLDISVW DYDIGKSNDY IGGCQLGISA
KGERLKHWYE CLKNKDKKIE RWHQLQNENH VSSD
//
MIM
612159
*RECORD*
*FIELD* NO
612159
*FIELD* TI
*612159 RABPHILIN 3A; RPH3A
;;KIAA0985
*FIELD* TX
DESCRIPTION
Exocytosis of neurotransmitters and hormones is fundamental to synaptic
read moreneurotransmission and cell-cell communication. RAB3A (179390) is a small
G protein that is thought to act at late stages of exocytosis, and RPH3A
is a RAB3A effector (Lin et al., 2007).
CLONING
By sequencing clones obtained from a size-fractionated brain cDNA
library, Nagase et al. (1999) cloned RPH3A, which they designated
KIAA0985. The deduced 694-amino acid protein shares 86.9% identity over
703 amino acids with rat Rph3a. RT-PCR ELISA detected highest expression
in fetal brain, followed by adult spinal cord and whole brain. Much
lower expression was detected in adult lung, testis, and spleen.
Expression was high in all specific adult brain regions tested, with
highest abundance in subthalamic nuclei and thalamus.
Inagaki et al. (1994) cloned mouse Rph3a, which encodes a deduced
681-amino acid protein with an N-terminal Rab3a-binding region and 2
C-terminal internal repeats homologous to the regulatory domain (C2
domain) of protein kinase C (see PRKCZ; 176982). Northern blot analysis
detected Rph3a highly expressed in brain and in several mammalian
endocrine and hormone-secreting cell lines.
GENE FUNCTION
Lin et al. (2007) found that direct interaction with rabphilin was
required for hydrolysis of GTP by Rab3a in stimulated rat
pheochromocytoma cells and for dissociation of Rab3a from vesicles and
exocytosis.
Smith et al. (2007) stated that the amount of Rph3a protein was reduced
in different brain regions in a transgenic mouse model of Huntington
disease (HD; 143100) and that Rph3a interacted with the SNARE synaptic
complex via Snap25 (600322). Western blot and immunohistochemical
analysis showed that levels of both SNAP25 and RPH3A were reduced in
human HD cortex. SNAP25 protein levels were lower even in HD brains with
limited neuropathology; the level of RPH3A deceased in HD brains with
higher neuropathologic grade and higher CAG repeats. The loss of SNAP25
and RPH3A was not due to general loss of synapses in HD cortex, since
the levels of other synapse-related proteins, including RAB3A, were
unaltered in the same patient samples.
MAPPING
By radiation hybrid analysis, Nagase et al. (1999) mapped the RPH3A gene
to chromosome 12.
*FIELD* RF
1. Inagaki, N.; Mizuta, M.; Seino, S.: Cloning of a mouse rabphilin-3A
expressed in hormone-secreting cells. J. Biochem. 116: 239-242,
1994.
2. Lin, C.-C.; Huang, C.-C.; Lin, K.-H.; Cheng, K.-H.; Yang, D.-M.;
Tsai, Y.-S.; Ong, R.-Y.; Huang, Y.-N.; Kao, L.-S.: Visualization
of Rab3A dissociation during exocytosis: a study by total internal
reflection microscopy. J. Cell. Physiol. 211: 316-326, 2007.
3. Nagase, T.; Ishikawa, K.; Suyama, M.; Kikuno, R.; Hirosawa, M.;
Miyajima, N.; Tanaka, A.; Kotani, H.; Nomura, N.; Ohara, O.: Prediction
of the coding sequences of unidentified human genes. XIII. The complete
sequences of 100 new cDNA clones from brain which code for large proteins
in vitro. DNA Res. 6: 63-70, 1999.
4. Smith, R.; Klein, P.; Koc-Schmitz, Y.; Waldvogel, H. J.; Faull,
R. L. M.; Brundin, P.; Plomann, M.; Li, J.-Y.: Loss of SNAP-25 and
rabphilin 3a in sensory-motor cortex in Huntington's disease. J.
Neurochem. 103: 115-123, 2007.
*FIELD* CD
Patricia A. Hartz: 7/2/2008
*FIELD* ED
wwang: 07/02/2008
*RECORD*
*FIELD* NO
612159
*FIELD* TI
*612159 RABPHILIN 3A; RPH3A
;;KIAA0985
*FIELD* TX
DESCRIPTION
Exocytosis of neurotransmitters and hormones is fundamental to synaptic
read moreneurotransmission and cell-cell communication. RAB3A (179390) is a small
G protein that is thought to act at late stages of exocytosis, and RPH3A
is a RAB3A effector (Lin et al., 2007).
CLONING
By sequencing clones obtained from a size-fractionated brain cDNA
library, Nagase et al. (1999) cloned RPH3A, which they designated
KIAA0985. The deduced 694-amino acid protein shares 86.9% identity over
703 amino acids with rat Rph3a. RT-PCR ELISA detected highest expression
in fetal brain, followed by adult spinal cord and whole brain. Much
lower expression was detected in adult lung, testis, and spleen.
Expression was high in all specific adult brain regions tested, with
highest abundance in subthalamic nuclei and thalamus.
Inagaki et al. (1994) cloned mouse Rph3a, which encodes a deduced
681-amino acid protein with an N-terminal Rab3a-binding region and 2
C-terminal internal repeats homologous to the regulatory domain (C2
domain) of protein kinase C (see PRKCZ; 176982). Northern blot analysis
detected Rph3a highly expressed in brain and in several mammalian
endocrine and hormone-secreting cell lines.
GENE FUNCTION
Lin et al. (2007) found that direct interaction with rabphilin was
required for hydrolysis of GTP by Rab3a in stimulated rat
pheochromocytoma cells and for dissociation of Rab3a from vesicles and
exocytosis.
Smith et al. (2007) stated that the amount of Rph3a protein was reduced
in different brain regions in a transgenic mouse model of Huntington
disease (HD; 143100) and that Rph3a interacted with the SNARE synaptic
complex via Snap25 (600322). Western blot and immunohistochemical
analysis showed that levels of both SNAP25 and RPH3A were reduced in
human HD cortex. SNAP25 protein levels were lower even in HD brains with
limited neuropathology; the level of RPH3A deceased in HD brains with
higher neuropathologic grade and higher CAG repeats. The loss of SNAP25
and RPH3A was not due to general loss of synapses in HD cortex, since
the levels of other synapse-related proteins, including RAB3A, were
unaltered in the same patient samples.
MAPPING
By radiation hybrid analysis, Nagase et al. (1999) mapped the RPH3A gene
to chromosome 12.
*FIELD* RF
1. Inagaki, N.; Mizuta, M.; Seino, S.: Cloning of a mouse rabphilin-3A
expressed in hormone-secreting cells. J. Biochem. 116: 239-242,
1994.
2. Lin, C.-C.; Huang, C.-C.; Lin, K.-H.; Cheng, K.-H.; Yang, D.-M.;
Tsai, Y.-S.; Ong, R.-Y.; Huang, Y.-N.; Kao, L.-S.: Visualization
of Rab3A dissociation during exocytosis: a study by total internal
reflection microscopy. J. Cell. Physiol. 211: 316-326, 2007.
3. Nagase, T.; Ishikawa, K.; Suyama, M.; Kikuno, R.; Hirosawa, M.;
Miyajima, N.; Tanaka, A.; Kotani, H.; Nomura, N.; Ohara, O.: Prediction
of the coding sequences of unidentified human genes. XIII. The complete
sequences of 100 new cDNA clones from brain which code for large proteins
in vitro. DNA Res. 6: 63-70, 1999.
4. Smith, R.; Klein, P.; Koc-Schmitz, Y.; Waldvogel, H. J.; Faull,
R. L. M.; Brundin, P.; Plomann, M.; Li, J.-Y.: Loss of SNAP-25 and
rabphilin 3a in sensory-motor cortex in Huntington's disease. J.
Neurochem. 103: 115-123, 2007.
*FIELD* CD
Patricia A. Hartz: 7/2/2008
*FIELD* ED
wwang: 07/02/2008