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CPLX3_HUMAN
ID   CPLX3_HUMAN             Reviewed;         158 AA.
AC   Q8WVH0; D3DW66; Q8TEM6; Q9H818;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Complexin-3;
DE   AltName: Full=Complexin III;
DE            Short=CPX III;
DE   Flags: Precursor;
GN   Name=CPLX3; ORFNames=Nbla11589;
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].
RC   TISSUE=Brain;
RX   PubMed=15911881; DOI=10.1083/jcb.200502115;
RA   Reim K., Wegmeyer H., Brandstaetter J.H., Xue M., Rosenmund C.,
RA   Dresbach T., Hofmann K., Brose N.;
RT   "Structurally and functionally unique complexins at retinal ribbon
RT   synapses.";
RL   J. Cell Biol. 169:669-680(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Spleen;
RA   Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
RT   "The nucleotide sequence of a long cDNA clone isolated from human spleen.";
RL   Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Neuroblastoma;
RX   PubMed=12880961; DOI=10.1016/s0304-3835(03)00085-5;
RA   Ohira M., Morohashi A., Nakamura Y., Isogai E., Furuya K., Hamano S.,
RA   Machida T., Aoyama M., Fukumura M., Miyazaki K., Suzuki Y., Sugano S.,
RA   Hirato J., Nakagawara A.;
RT   "Neuroblastoma oligo-capping cDNA project: toward the understanding of the
RT   genesis and biology of neuroblastoma.";
RL   Cancer Lett. 197:63-68(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Complexin that regulates SNARE protein complex-mediated
CC       synaptic vesicle fusion (By similarity). Required for the maintenance
CC       of synaptic ultrastructure in the adult retina (By similarity).
CC       Positively regulates synaptic transmission through synaptic vesicle
CC       availability and exocytosis of neurotransmitters at photoreceptor
CC       ribbon synapses in the retina (By similarity). Suppresses tonic
CC       photoreceptor activity and baseline 'noise' by suppression of Ca(2+)
CC       vesicle tonic release and the facilitation of evoked synchronous and
CC       asynchronous Ca(2+) vesicle release (By similarity).
CC       {ECO:0000250|UniProtKB:Q8R1B5}.
CC   -!- SUBUNIT: Binds to the SNARE core complex containing SNAP25, VAMP2 and
CC       STX1A. {ECO:0000250|UniProtKB:Q8R1B5}.
CC   -!- SUBCELLULAR LOCATION: Synapse {ECO:0000250|UniProtKB:Q8R1B5}. Cell
CC       membrane; Lipid-anchor {ECO:0000250|UniProtKB:Q8R1B5}. Note=Enriched at
CC       the synaptic terminal (By similarity). Localized at glycinergic
CC       synaptic contacts of AII amacrine cells with OFF cone bipolar cells in
CC       the OFF sublamina of the retina inner nuclear layer (By similarity).
CC       {ECO:0000250|UniProtKB:Q8R1B5}.
CC   -!- PTM: Farnesylation mediates presynaptic targeting.
CC       {ECO:0000250|UniProtKB:Q8R1B5}.
CC   -!- SIMILARITY: Belongs to the complexin/synaphin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB84922.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AY286501; AAP41127.1; -; mRNA.
DR   EMBL; AK074096; BAB84922.1; ALT_INIT; mRNA.
DR   EMBL; AB072900; BAE45711.1; -; mRNA.
DR   EMBL; AK024055; BAB14805.1; -; mRNA.
DR   EMBL; CH471136; EAW99306.1; -; Genomic_DNA.
DR   EMBL; CH471136; EAW99307.1; -; Genomic_DNA.
DR   EMBL; BC018026; AAH18026.1; -; mRNA.
DR   CCDS; CCDS32294.1; -.
DR   RefSeq; NP_001025176.1; NM_001030005.2.
DR   AlphaFoldDB; Q8WVH0; -.
DR   SMR; Q8WVH0; -.
DR   BioGRID; 534761; 26.
DR   CORUM; Q8WVH0; -.
DR   IntAct; Q8WVH0; 17.
DR   STRING; 9606.ENSP00000378464; -.
DR   GlyGen; Q8WVH0; 1 site, 1 O-linked glycan (1 site).
DR   PhosphoSitePlus; Q8WVH0; -.
DR   BioMuta; CPLX3; -.
DR   DMDM; 74751549; -.
DR   MassIVE; Q8WVH0; -.
DR   PaxDb; Q8WVH0; -.
DR   PeptideAtlas; Q8WVH0; -.
DR   PRIDE; Q8WVH0; -.
DR   ProteomicsDB; 74793; -.
DR   Antibodypedia; 43203; 142 antibodies from 22 providers.
DR   DNASU; 594855; -.
DR   Ensembl; ENST00000395018.6; ENSP00000378464.4; ENSG00000213578.6.
DR   GeneID; 594855; -.
DR   KEGG; hsa:594855; -.
DR   MANE-Select; ENST00000395018.6; ENSP00000378464.4; NM_001030005.3; NP_001025176.1.
DR   UCSC; uc059llo.1; human.
DR   CTD; 594855; -.
DR   GeneCards; CPLX3; -.
DR   HGNC; HGNC:27652; CPLX3.
DR   HPA; ENSG00000213578; Group enriched (lymphoid tissue, prostate, retina).
DR   MIM; 609585; gene.
DR   neXtProt; NX_Q8WVH0; -.
DR   OpenTargets; ENSG00000213578; -.
DR   PharmGKB; PA142672081; -.
DR   VEuPathDB; HostDB:ENSG00000213578; -.
DR   eggNOG; ENOG502QZ0D; Eukaryota.
DR   GeneTree; ENSGT00950000182938; -.
DR   HOGENOM; CLU_141096_0_0_1; -.
DR   InParanoid; Q8WVH0; -.
DR   OMA; QSAEKCY; -.
DR   OrthoDB; 1441014at2759; -.
DR   PhylomeDB; Q8WVH0; -.
DR   TreeFam; TF331867; -.
DR   PathwayCommons; Q8WVH0; -.
DR   SignaLink; Q8WVH0; -.
DR   BioGRID-ORCS; 594855; 13 hits in 1064 CRISPR screens.
DR   GenomeRNAi; 594855; -.
DR   Pharos; Q8WVH0; Tbio.
DR   PRO; PR:Q8WVH0; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; Q8WVH0; protein.
DR   Bgee; ENSG00000213578; Expressed in spleen and 66 other tissues.
DR   ExpressionAtlas; Q8WVH0; baseline.
DR   Genevisible; Q8WVH0; HS.
DR   GO; GO:0099029; C:anchored component of presynaptic active zone membrane; IEA:Ensembl.
DR   GO; GO:0098993; C:anchored component of synaptic vesicle membrane; IEA:Ensembl.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0098684; C:photoreceptor ribbon synapse; IEA:Ensembl.
DR   GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR   GO; GO:0043195; C:terminal bouton; IBA:GO_Central.
DR   GO; GO:0005326; F:neurotransmitter transmembrane transporter activity; IEA:Ensembl.
DR   GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR   GO; GO:0019905; F:syntaxin binding; IEA:InterPro.
DR   GO; GO:0030073; P:insulin secretion; IEA:Ensembl.
DR   GO; GO:0046928; P:regulation of neurotransmitter secretion; IBA:GO_Central.
DR   GO; GO:0031630; P:regulation of synaptic vesicle fusion to presynaptic active zone membrane; IEA:Ensembl.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR   GO; GO:0016079; P:synaptic vesicle exocytosis; IBA:GO_Central.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR   InterPro; IPR008849; Synaphin.
DR   PANTHER; PTHR16705; PTHR16705; 1.
DR   Pfam; PF05835; Synaphin; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Coiled coil; Exocytosis; Lipoprotein; Membrane; Methylation;
KW   Neurotransmitter transport; Prenylation; Reference proteome;
KW   Sensory transduction; Synapse; Transport; Vision.
FT   CHAIN           1..155
FT                   /note="Complexin-3"
FT                   /id="PRO_0000239272"
FT   PROPEP          156..158
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000240233"
FT   REGION          13..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          74..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          39..74
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        24..47
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         155
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R1B5"
FT   LIPID           155
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R1B5"
FT   CONFLICT        19
FT                   /note="S -> G (in Ref. 4; BAB14805)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   158 AA;  17557 MW;  057B4DE06DB6EA0F CRC64;
     MAFMVKTMVG GQLKNLTGSL GGGEDKGDGD KSAAEAQGMS REEYEEYQKQ LVEEKMERDA
     QFTQRKAERA TLRSHFRDKY RLPKNETDES QIQMAGGDVE LPRELAKMIE EDTEEEEEKA
     SVLGQLASLP GLNLGSLKDK AQATLGDLKQ SAEKCHVM
 
 
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