ID A0A3B3D5L9_ORYME Unreviewed; 502 AA.
AC A0A3B3D5L9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Protein kinase C and casein kinase substrate in neurons 2 {ECO:0000313|Ensembl:ENSOMEP00000024764.1};
OS Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000024764.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000024764.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000256|ARBA:ARBA00004412}.
CC Endosome {ECO:0000256|ARBA:ARBA00004177}.
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DR AlphaFoldDB; A0A3B3D5L9; -.
DR STRING; 30732.ENSOMEP00000024764; -.
DR PaxDb; 30732-ENSOMEP00000024764; -.
DR Ensembl; ENSOMET00000008841.1; ENSOMEP00000024764.1; ENSOMEG00000005606.1.
DR GeneTree; ENSGT00950000182973; -.
DR Proteomes; UP000261560; Unplaced.
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; 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; 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 4: Predicted;
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 Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 10..281
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 443..502
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 331..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 186..217
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 339..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..418
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 502 AA; 57836 MW; 10CA4EB6636B920F CRC64;
MSGSCEDSMI DVSSDSFWEV GNYKRTVKRV DDGHRLCNDL MTCLHERARI EKTYAQQLTE
WGKRWRQLIE KGPQYGSLER AWAALCTEAE KVSELHMEVK AQLMGEDYEK LKNWQKDSYH
KQMIGGFKET KEADDGFRKA QKPWAKKLKE VDTMKKAYHA ACKEEKLATS RESNSKLESN
NNPETLKKLQ EKVEKCQQEV QKTKERYEKS LEELDKLTPQ YMENMEQVFE QLQQFEDKRI
CFFKELLLEV KQHLDLSTNH RFQTVYQTLE DTLTATDAEE DLKWFRFNHG PGMPMNWPQF
ETLDVSHPAS FRRRSILDWS IDINRTLSRR EKKKPEGVTL TGINQTGADQ PVQPTKTSNS
LTVPTNAAPA GSNPFEEDED EEEEEAAQEH KAPVVSIRVN KEEIKTASST EKTPDWSDED
TVGNPFATNG DGNPFEEEPA SPLISVPVKA LYDYEGQEQD ELSFKSGDEF TKIGVEDDQG
WCKGRLKDGH VGLYPANYVE EI
//