ID A0A0R4IHF0_DANRE Unreviewed; 491 AA. AC A0A0R4IHF0; A0A8M2BFX2; DT 20-JUN-2018, integrated into UniProtKB/TrEMBL. DT 20-JUN-2018, sequence version 1. DT 27-MAR-2024, entry version 33. DE SubName: Full=Protein kinase C and casein kinase substrate in neurons 2 {ECO:0000313|Ensembl:ENSDARP00000133109}; DE SubName: Full=Protein kinase C and casein kinase substrate in neurons protein 2 isoform X1 {ECO:0000313|RefSeq:XP_005168648.1}; GN Name=pacsin2 {ECO:0000313|Ensembl:ENSDARP00000133109, GN ECO:0000313|RefSeq:XP_005168648.1, GN ECO:0000313|ZFIN:ZDB-GENE-040426-2596}; GN Synonyms=zgc:77519 {ECO:0000313|RefSeq:XP_005168648.1}; 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|Ensembl:ENSDARP00000133109}; RN [1] {ECO:0000313|Ensembl:ENSDARP00000133109, ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000133109}; 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 [2] {ECO:0000313|Ensembl:ENSDARP00000133109} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000133109}; RG Ensembl; RL Submitted (NOV-2015) to UniProtKB. RN [3] {ECO:0000313|RefSeq:XP_005168648.1} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:XP_005168648.1}; RG RefSeq; RL Submitted (NOV-2023) to UniProtKB. CC -!- SUBCELLULAR LOCATION: Cell projection, ruffle membrane CC {ECO:0000256|ARBA:ARBA00004599}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004599}; Cytoplasmic side CC {ECO:0000256|ARBA:ARBA00004599}. Early endosome CC {ECO:0000256|ARBA:ARBA00004412}. Endosome membrane CC {ECO:0000256|ARBA:ARBA00004608}. Membrane, caveola CC {ECO:0000256|ARBA:ARBA00004345}. Recycling endosome membrane CC {ECO:0000256|ARBA:ARBA00004565}. CC -!- SIMILARITY: Belongs to the PACSIN family. CC {ECO:0000256|ARBA:ARBA00010461}. 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; CU694238; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CU695158; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_005168648.1; XM_005168591.4. DR Ensembl; ENSDART00000159094; ENSDARP00000133109; ENSDARG00000078014. DR Ensembl; ENSDART00000159094.2; ENSDARP00000133109.2; ENSDARG00000078014.4. DR GeneID; 404601; -. DR AGR; ZFIN:ZDB-GENE-040426-2596; -. DR CTD; 11252; -. DR ZFIN; ZDB-GENE-040426-2596; pacsin2. DR OMA; PDSLGWC; -. DR OrthoDB; 9421at2759; -. DR Reactome; R-DRE-8856828; Clathrin-mediated endocytosis. DR Proteomes; UP000000437; Chromosome 4. DR Bgee; ENSDARG00000078014; Expressed in granulocyte and 33 other cell types or tissues. DR GO; GO:0005901; C:caveola; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell. DR GO; GO:0005768; C:endosome; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central. DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro. DR GO; GO:0070836; P:caveola assembly; IEA:InterPro. DR GO; GO:0060271; P:cilium assembly; IGI:ZFIN. DR GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central. 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; IMP:ZFIN. DR CDD; cd07679; F-BAR_PACSIN2; 1. DR CDD; cd11843; SH3_PACSIN; 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; IPR037453; PACSIN2_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:SF14; PROTEIN KINASE C AND CASEIN KINASE SUBSTRATE IN NEURONS PROTEIN 2; 1. DR Pfam; PF00611; FCH; 1. DR Pfam; PF14604; SH3_9; 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 {ECO:0000256|ARBA:ARBA00022475}; KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE- KW ProRule:PRU01077}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Kinase {ECO:0000313|RefSeq:XP_005168648.1}; KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A0R4IHF0}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE- KW ProRule:PRU00192}; Transferase {ECO:0000313|RefSeq:XP_005168648.1}. FT DOMAIN 9..279 FT /note="F-BAR" FT /evidence="ECO:0000259|PROSITE:PS51741" FT DOMAIN 431..491 FT /note="SH3" FT /evidence="ECO:0000259|PROSITE:PS50002" FT REGION 161..186 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 310..430 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 326..346 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 352..366 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 491 AA; 56216 MW; 36E76FC3463A4F78 CRC64; MSDFNDSLID VSSDSFWEVG NYKRSVKRVD DGNRLCNDLM SCLHERARIE KSYSTQLTDW AKRWRQTIEK GPQYGTVERA WCALMTEAEK VSDLHMEVKA ALMAEDFEKI KNWQKDAYHK QMIGGFKETK EAEDGFRKAQ KPWAKKLKEM ETMKKAYHTA CKEEKTATSR ENSSKLDNSN PEAQKKLQEK VEKCQQEVQK TKERYEKSLE DLDKVTPQYM ENMEQVFEQW QQFEGKRLSF FKEVLLEVKQ HLDLSSNHKY TTVYHTLQDT IQGADPQEDL KWFRSNHGPG MTMNWPQFEE WSMDLNRTLS RRETKRRPAE GVTLTAISHN PEQSSRVSSV PAVSSSEAAC LNPFDDDDDD EDEDEEPVVT HTHSSPVKHE EAVAQTSAAV EKAPAPAAIT AADDDDDEES GNPFSSSSAN GNPFEEEPST EMCVPVRAVY DYEGQEQDEL SFKAGDELVK LSEEDEQGWC KGRLSNGTVG LYPANYVEDL Q //