CAPS1_XENLA
ID CAPS1_XENLA Reviewed; 1299 AA.
AC Q6GLR7;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Calcium-dependent secretion activator 1;
DE AltName: Full=Calcium-dependent activator protein for secretion 1;
DE Short=CAPS-1;
GN Name=cadps; Synonyms=caps, caps1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Calcium-binding protein involved in exocytosis of vesicles
CC filled with neurotransmitters and neuropeptides. Probably acts upstream
CC of fusion in the biogenesis or maintenance of mature secretory
CC vesicles. Regulates catecholamine loading of DCVs. May specifically
CC mediate the Ca(2+)-dependent exocytosis of large dense-core vesicles
CC (DCVs) (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Synapse {ECO:0000250|UniProtKB:Q62717}.
CC Cytoplasmic vesicle, secretory vesicle, neuronal dense core vesicle
CC membrane {ECO:0000250|UniProtKB:Q62717}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q62717}. Note=Membrane-associated to vesicles.
CC Strongly enriched in synaptic fractions. Preferentially binds to DCVs
CC but not to SVs. Binds phosphoinosides. {ECO:0000250|UniProtKB:Q62717}.
CC -!- DOMAIN: The PH domain is essential for regulated exocytosis and binds
CC phospholipids. {ECO:0000250}.
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DR EMBL; BC074390; AAH74390.1; -; mRNA.
DR RefSeq; NP_001086256.1; NM_001092787.1.
DR AlphaFoldDB; Q6GLR7; -.
DR SMR; Q6GLR7; -.
DR MaxQB; Q6GLR7; -.
DR GeneID; 444685; -.
DR KEGG; xla:444685; -.
DR CTD; 444685; -.
DR Xenbase; XB-GENE-5755962; cadps.L.
DR OrthoDB; 138870at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 444685; Expressed in brain and 6 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0099012; C:neuronal dense core vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1990504; P:dense core granule exocytosis; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; IEA:InterPro.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR033227; CAPS.
DR InterPro; IPR010439; MUN_dom.
DR InterPro; IPR014770; Munc13_1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR12166; PTHR12166; 1.
DR Pfam; PF06292; MUN; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM01145; DUF1041; 1.
DR SMART; SM00233; PH; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS51258; MHD1; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 2: Evidence at transcript level;
KW Calcium; Cytoplasmic vesicle; Exocytosis; Lipid-binding; Membrane;
KW Metal-binding; Protein transport; Reference proteome; Synapse; Transport.
FT CHAIN 1..1299
FT /note="Calcium-dependent secretion activator 1"
FT /id="PRO_0000053867"
FT DOMAIN 347..462
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 488..591
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 891..1068
FT /note="MHD1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00587"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1277..1299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1299 AA; 148720 MW; FED4CA3940D6486D CRC64;
MLDPSSSEEE AEEVVEEPEI KEGQAPTTGT RLSPSRTSES SGGLQPSSRS SSVRPSSPSP
SVVSEKEKEE LEKLQKEEEE RKRKLQLYVF VMRCIAYPFN AKQPTDMARR QQKISKQQLQ
TVKDRFQAFF NGETQIVADE AFMNAVQSYY EVFLKSDRVA RMVQSGGCSA NDSREVFKKH
IEKRVRSLPE IDGLSKETVL SSWIAKFDAI YRGEEDPRKQ QARMTASAAS ELILSKEQLY
EMFQQILGIK KFEHQLLYNA CQLDNLDEQA AQIRRELDGR LQMADQIARE RKFPKFVSKE
MENMYIEELK SSVNLLMANL ESMPVSKGGS EFKLQKLKRS HNTSIIDMGE ENENQLSKSD
VVLSFSLEVV IMEVQGLKSL APNRIVYCTM EVEGGQKLQT DQAEASKPMW GTQGDFSTTH
ALPAVKVKLF TESTGVLALE DKELGRVVLH PTPNSPKQSE WHKMTVSKNC PDHDLKIKLA
VRMDKPQNMK HCGYLWVIGK NVWKRWKKRF FVLVQVSQYT FAMCSYREKK AEPQELLQLD
GYTVDYTDPQ PGLEGGRSFF NAVKEGDTVI FASDDEQDRI LWVQAMYRAT GQSHKPVPPT
QVQKLNAKGG NIPQLDAPIS QFYADRAQKH GMDEFISSNP CNFDHATLFE MVQRLTLDHR
LNDSYSCLGW FSPGQVFVLD EYCARYGVRG CHRHLCYLGD LLERAENGSM VDPTLLHYSF
AFCASHVHGN RPDGIGTVTV EEKERFEEIK ERLRLLLENQ ITHFRYCFPF GRPEGALKAT
LSLLERVLMK DIVTPVPQED VKNVIRKCLE QAALVNYTRL SEYAKIEENQ KDAENVGRLI
TPAKKLEDTI RLAELVIEVL QQNEEHHAEA FAWWSDLMVE HAETFLSLFA VDMDAALEVQ
PPDSWESFPL FQLINDFLRS DYNLCNGKFH KHLQDLFAPL VVRYVDLMES SIAQSIHRGF
ERESWEPVKS LTSNLPNVNL PNVNLPKVPV TLPVNLPQMP SFSAPSWMAA IYDSDNGSAT
SEDLFWKLDA LQTFIRDLHW PEEEFGKHLE QRLKLMASDM IESCVKRTRI AFEVKLQKTS
RSTDFRVPQS ICTMFNVMVD AKAQSTKLCS MEMGQEHQYH SKIDELIEET VKEMITLLVA
KFVTILEGVL SKLSRYDEGT LFSSFLSFTK PGMDLADAYV TFIRHSQDVL RDKVNEEIYI
ERLFDQWYTS SMNVVCTWLT DRMDLQLHIY QLKTLIRIVK KTYRDFRLQG VLDSTLNSKT
YDTVRNRLTV EEATASVSEG GGLQGITMKD SDEEDEEDD
