ID PACN1_DANRE Reviewed; 445 AA.
AC Q4V920;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 130.
DE RecName: Full=Protein kinase C and casein kinase substrate in neurons protein 1;
DE AltName: Full=Syndapin-1;
GN Name=pacsin1b; Synonyms=pacsin1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH COBL, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=23203810; DOI=10.1242/jcs.111674;
RA Schuler S., Hauptmann J., Perner B., Kessels M.M., Englert C., Qualmann B.;
RT "Ciliated sensory hair cell formation and function require the F-BAR
RT protein syndapin I and the WH2 domain-based actin nucleator Cobl.";
RL J. Cell Sci. 126:196-208(2013).
CC -!- FUNCTION: Binds to membranes via its F-BAR domain and mediates membrane
CC tubulation. Plays a role in cellular transport processes by recruiting
CC dynamins to membranes. Plays a role in the reorganization of the actin
CC cytoskeleton and in neuron morphogenesis via its interaction with cobl,
CC and by recruiting cobl to the cell cortex. Plays a role in the
CC regulation of neurite formation, neurite branching and the regulation
CC of neurite length. Required for normal synaptic vesicle endocytosis;
CC this process retrieves previously released neurotransmitters to
CC accommodate multiple cycles of neurotransmission. Required for normal
CC excitatory and inhibitory synaptic transmission (By similarity).
CC Required for normal embryonic development, including normal development
CC of laterality, normal body size and shape, as well as normal brain and
CC heart development. Required for normal development of stereocilia and
CC kinocilia in sensory hair cells of neuromasts in the posterior lateral
CC line organ, and thus also for balance keeping and normal swimming
CC behavior. {ECO:0000250, ECO:0000269|PubMed:23203810}.
CC -!- SUBUNIT: Interacts with cobl. {ECO:0000269|PubMed:23203810}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23203810}.
CC Cytoplasm, cytosol {ECO:0000269|PubMed:23203810}. Cell membrane
CC {ECO:0000269|PubMed:23203810}; Peripheral membrane protein
CC {ECO:0000269|PubMed:23203810}; Cytoplasmic side
CC {ECO:0000269|PubMed:23203810}. Cell projection {ECO:0000250}. Synapse,
CC synaptosome {ECO:0000250}. Synapse {ECO:0000250}. Cytoplasmic vesicle
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell
CC projection, ruffle membrane {ECO:0000250}. Membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Note=Detected in axons. In
CC primary neuronal cultures, present at a high level in presynaptic nerve
CC terminals and in the cell body. Detected at vesicular structures in
CC neuron cell bodies and neurites (By similarity). Detected at the apical
CC surface of cells at the basis of forming cilia, but not in the cilia
CC themselves. {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed throughout embryogenesis, from
CC fertilization to hatching. Detected in embryonic neuronal tissues,
CC including forebrain, hindbrain, spinal cord and retina.
CC {ECO:0000269|PubMed:23203810}.
CC -!- DOMAIN: The F-BAR domain mediates membrane-binding and membrane
CC tubulation. {ECO:0000250}.
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DR EMBL; CU694224; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU855791; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU855800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU914470; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC097107; AAH97107.1; -; mRNA.
DR RefSeq; NP_001028900.1; NM_001033728.1.
DR RefSeq; XP_005166197.1; XM_005166140.2.
DR RefSeq; XP_009301003.1; XM_009302728.2.
DR AlphaFoldDB; Q4V920; -.
DR SMR; Q4V920; -.
DR STRING; 7955.ENSDARP00000056829; -.
DR PaxDb; 7955-ENSDARP00000107643; -.
DR GeneID; 619246; -.
DR KEGG; dre:619246; -.
DR AGR; ZFIN:ZDB-GENE-050913-35; -.
DR CTD; 619246; -.
DR ZFIN; ZDB-GENE-050913-35; pacsin1b.
DR eggNOG; KOG2856; Eukaryota.
DR HOGENOM; CLU_030752_0_0_1; -.
DR InParanoid; Q4V920; -.
DR OMA; EGGNTYN; -.
DR OrthoDB; 9421at2759; -.
DR PhylomeDB; Q4V920; -.
DR TreeFam; TF313677; -.
DR Reactome; R-DRE-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:Q4V920; -.
DR Proteomes; UP000000437; Chromosome 6.
DR Bgee; ENSDARG00000042128; Expressed in intestine and 28 other cell types or tissues.
DR ExpressionAtlas; Q4V920; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR GO; GO:0060088; P:auditory receptor cell stereocilium organization; IMP:ZFIN.
DR GO; GO:0060271; P:cilium assembly; IGI:ZFIN.
DR GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
DR GO; GO:0097320; P:plasma membrane tubulation; IBA:GO_Central.
DR GO; GO:1900006; P:positive regulation of dendrite development; IBA:GO_Central.
DR GO; GO:0030100; P:regulation of endocytosis; IBA:GO_Central.
DR CDD; cd07680; F-BAR_PACSIN1; 1.
DR CDD; cd11998; SH3_PACSIN1-2; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR035743; PACSIN1/PACSIN2_SH3.
DR InterPro; IPR037454; PACSIN1_F-BAR.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR23065; PROLINE-SERINE-THREONINE PHOSPHATASE INTERACTING PROTEIN 1; 1.
DR PANTHER; PTHR23065:SF16; PROTEIN KINASE C AND CASEIN KINASE SUBSTRATE IN NEURONS PROTEIN 1; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Endocytosis; Lipid-binding; Membrane;
KW Reference proteome; SH3 domain; Synapse; Synaptosome.
FT CHAIN 1..445
FT /note="Protein kinase C and casein kinase substrate in
FT neurons protein 1"
FT /id="PRO_0000422220"
FT DOMAIN 12..282
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 386..445
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 327..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 146..167
FT /evidence="ECO:0000250"
FT COILED 183..219
FT /evidence="ECO:0000250"
FT COMPBIAS 327..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 445 AA; 51356 MW; 53552263222290C5 CRC64;
MSGAYDESAM SDETTDSFWE VGNYKRTVKR IEDGHRLCND MMSCIQERAK IEKAYSQQLT
DWSKRWRQLV ERGPQYGTLE RAWLAVMTEA EKVSELHQEV KNNLLNEDLE KVKNWQKDAY
HKQMMGGFKE TKEADEGFRK AQKPWAKKLK ELETAKKTYH MACKEEKIAS AREANSKGEA
SVTTDQQKKL QEKVDKCKND VQKAKEKYEK SLDELNKCTP QYMENMEVVF DQCQQFEEKR
LNFLREVLLD TKRHLNLTES QSYATVYREL ERTIVSASAQ EDLKWFSSVH GPGMHMNWPQ
FEEFNPDLSH AISKKEKVKR NHDGVTLTQV THGAEHGTPQ TGDRGSVSSY EKNQQYSAEW
SDDEQPPTAA QSASETNGGN PFEEDSKGVR VRALYDYEGQ EQDELTFKAG DELTKLEDED
EQGWCKGRLD SGQLGLYPAN YVEPV
//
