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Database: UniProt
Entry: A0A3B3D5L9_ORYME
LinkDB: A0A3B3D5L9_ORYME
Original site: A0A3B3D5L9_ORYME 
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
//
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