ID U3JUW2_FICAL Unreviewed; 457 AA.
AC U3JUW2;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Protein kinase C and casein kinase substrate in neurons 3 {ECO:0000313|Ensembl:ENSFALP00000006566.1};
GN Name=PACSIN3 {ECO:0000313|Ensembl:ENSFALP00000006566.1};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000006566.1, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000006566.1, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000006566.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR RefSeq; XP_005047156.1; XM_005047099.2.
DR AlphaFoldDB; U3JUW2; -.
DR STRING; 59894.ENSFALP00000006566; -.
DR Ensembl; ENSFALT00000006595.2; ENSFALP00000006566.1; ENSFALG00000006296.2.
DR GeneID; 101813418; -.
DR KEGG; fab:101813418; -.
DR CTD; 29763; -.
DR eggNOG; KOG2856; Eukaryota.
DR GeneTree; ENSGT00950000182973; -.
DR HOGENOM; CLU_030752_0_0_1; -.
DR OMA; DRVEKCS; -.
DR OrthoDB; 9421at2759; -.
DR Proteomes; UP000016665; Chromosome 5.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0019855; F:calcium channel inhibitor activity; IEA:Ensembl.
DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0008289; F:lipid binding; IEA:Ensembl.
DR GO; GO:0051926; P:negative regulation of calcium ion transport; IEA:Ensembl.
DR GO; GO:0045806; P:negative regulation of endocytosis; IEA:Ensembl.
DR GO; GO:0097320; P:plasma membrane tubulation; IEA:Ensembl.
DR GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IEA:Ensembl.
DR CDD; cd11997; SH3_PACSIN3; 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; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
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 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 4: Predicted;
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01077};
KW Reference proteome {ECO:0000313|Proteomes:UP000016665};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 10..280
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 396..457
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 154..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 457 AA; 53010 MW; 69652E2A10CD3B7F CRC64;
MSSEDDAGGE APGGSFWEAG NYKRTVKRVD DGYRLCNDLI SCFQERAKIE KNYAQQLTEW
SRKWRTNVER GPQYGTLEKA WHAFLTAADK LSEIHLAVRN HLAGEDSDKI KAWQKEAYHK
QMIGGFKETK DAEDGFRKAQ KPWVKKMKDV ETSKKNYHAA RKEEKTAHTR ENHAKADSSV
SQEQMRKLQE RVEKCTQEAE KCKDQYEKML EELNRYNPRY MEDMEQVFEG CQEAERKRLC
FFKEMLLNLH QHLNLSTSES FHALYRDLHQ VIMAADNQED LKWWRNTHGP GMAMNWPQFE
EWSLETQRQI TKKEKSGKMA DDVTLTSILP TRDGVVSQTP LQTRFSYQEE QNSLFYDTLK
APTHVNGGKE DISEWSDEDT PKKCLDANGH EEDLKVPGVR VRALYDYTGQ EADELSFKAG
EELMKISEED EQGWCKGRLL TGQVGLYPAN YVEKVGS
//
