ID Q7ZUY8_DANRE Unreviewed; 377 AA.
AC Q7ZUY8; A0A8N1Z331;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 132.
DE SubName: Full=Protein kinase C and casein kinase substrate in neurons 3 {ECO:0000313|Ensembl:ENSDARP00000131278};
DE SubName: Full=Protein kinase C and casein kinase substrate in neurons protein 3 {ECO:0000313|RefSeq:NP_957283.1};
DE SubName: Full=Zgc:56324 {ECO:0000313|EMBL:AAH46073.1};
GN Name=pacsin3 {ECO:0000313|Ensembl:ENSDARP00000131278,
GN ECO:0000313|RefSeq:NP_957283.1, ECO:0000313|ZFIN:ZDB-GENE-040426-984};
GN Synonyms=fa11d03 {ECO:0000313|RefSeq:NP_957283.1}, fj67e09
GN {ECO:0000313|RefSeq:NP_957283.1}, Pacsin1
GN {ECO:0000313|RefSeq:NP_957283.1}, wu:fa11d03
GN {ECO:0000313|RefSeq:NP_957283.1}, wu:fj67e09
GN {ECO:0000313|RefSeq:NP_957283.1}, wu:fq16a06
GN {ECO:0000313|RefSeq:NP_957283.1}, zgc:56324
GN {ECO:0000313|RefSeq:NP_957283.1};
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 {ECO:0000313|EMBL:AAH46073.1};
RN [1] {ECO:0000313|EMBL:AAH46073.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Whole body {ECO:0000313|EMBL:AAH46073.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|RefSeq:NP_957283.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=19997509; DOI=10.1371/journal.pone.0008150;
RA Edeling M.A., Sanker S., Shima T., Umasankar P.K., Honing S., Kim H.Y.,
RA Davidson L.A., Watkins S.C., Tsang M., Owen D.J., Traub L.M.;
RT "Structural requirements for PACSIN/Syndapin operation during zebrafish
RT embryonic notochord development.";
RL PLoS ONE 4:e8150-e8150(2009).
RN [3] {ECO:0000313|Ensembl:ENSDARP00000131278, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000131278};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
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., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA 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 [4] {ECO:0000313|RefSeq:NP_957283.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25840431;
RA Manchenkov T., Pasillas M.P., Haddad G.G., Imam F.B.;
RT "Novel Genes Critical for Hypoxic Preconditioning in Zebrafish Are
RT Regulators of Insulin and Glucose Metabolism.";
RL G3 (Bethesda) 5:1107-1116(2015).
RN [5] {ECO:0000313|Ensembl:ENSDARP00000131278}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000131278};
RG Ensembl;
RL Submitted (NOV-2015) to UniProtKB.
RN [6] {ECO:0000313|RefSeq:NP_957283.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=27189481;
RA Pasquier J., Cabau C., Nguyen T., Jouanno E., Severac D., Braasch I.,
RA Journot L., Pontarotti P., Klopp C., Postlethwait J.H., Guiguen Y.,
RA Bobe J.;
RT "Gene evolution and gene expression after whole genome duplication in fish:
RT the PhyloFish database.";
RL BMC Genomics 17:368-368(2016).
RN [7] {ECO:0000313|RefSeq:NP_957283.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=28252024;
RA Bayes A., Collins M.O., Reig-Viader R., Gou G., Goulding D., Izquierdo A.,
RA Choudhary J.S., Emes R.D., Grant S.G.;
RT "Evolution of complexity in the zebrafish synapse proteome.";
RL Nat. Commun. 8:14613-14613(2017).
RN [8] {ECO:0000313|RefSeq:NP_957283.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL935050; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU928764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC046073; AAH46073.1; -; mRNA.
DR RefSeq; NP_957283.1; NM_200989.1.
DR STRING; 7955.ENSDARP00000131278; -.
DR PaxDb; 7955-ENSDARP00000089068; -.
DR Ensembl; ENSDART00000165201.3; ENSDARP00000131278.1; ENSDARG00000099339.4.
DR GeneID; 393964; -.
DR KEGG; dre:393964; -.
DR AGR; ZFIN:ZDB-GENE-040426-984; -.
DR CTD; 29763; -.
DR ZFIN; ZDB-GENE-040426-984; pacsin3.
DR eggNOG; KOG2856; Eukaryota.
DR HOGENOM; CLU_030752_2_0_1; -.
DR OrthoDB; 9421at2759; -.
DR TreeFam; TF313677; -.
DR Proteomes; UP000000437; Chromosome 7.
DR Bgee; ENSDARG00000099339; Expressed in bone element and 43 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:ZFIN.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0060034; P:notochord cell differentiation; IMP:ZFIN.
DR GO; GO:0014028; P:notochord formation; IMP:ZFIN.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0097320; P:plasma membrane tubulation; IBA:GO_Central.
DR GO; GO:0030100; P:regulation of endocytosis; IBA:GO_Central.
DR CDD; cd07681; F-BAR_PACSIN3; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR PANTHER; PTHR23065; PROLINE-SERINE-THREONINE PHOSPHATASE INTERACTING PROTEIN 1; 1.
DR PANTHER; PTHR23065:SF18; PROTEIN KINASE C AND CASEIN KINASE SUBSTRATE IN NEURONS PROTEIN 3; 1.
DR Pfam; PF00611; FCH; 1.
DR SMART; SM00055; FCH; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR PROSITE; PS51741; F_BAR; 1.
PE 1: Evidence at protein level;
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01077, ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000313|RefSeq:NP_957283.1};
KW Proteomics identification {ECO:0007829|PeptideAtlas:Q7ZUY8};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW Transferase {ECO:0000313|RefSeq:NP_957283.1}.
FT DOMAIN 8..280
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT REGION 155..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 185..216
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 330..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 377 AA; 44196 MW; 1181475AF96AFF60 CRC64;
MSSNGDLQDV GSWDSFWEPG NYKRTVKRID DGYKLCNELV SCFQERAKIE KGYSQQLSDW
ARKWRGIVEK GSQYGTLEKA WHAFMNAADR LSEIHMELKE NLVIEDSEKI RNWQKDAFHK
QMIGGFRETK DADEGFRKAQ KPWVRKLKEV ESTKKGYHSA RKEERTALTR ETHAKADPTK
SQDEVRKFTD RLEKCTQEAE KAKERYERAL DELNRCNPRY MEDMEQVFEI TQEAEKNRLC
FFKEVLLDIH QHMDLSSNDR FRALYRDLGQ TISAANDTED LRWWRNTHGP GMSMNWPQFE
EWSPEANRSI SRKDRNSRSD DVVTLTNIVS AGDEPPQTLQ ETTRAGKDYS SDWSDEESPK
KYIAANGVDE EEKEKSC
//
