ID A0A1S3N1T9_SALSA Unreviewed; 496 AA.
AC A0A1S3N1T9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Protein kinase C and casein kinase substrate in neurons protein 2-like isoform X2 {ECO:0000313|RefSeq:XP_014008981.1};
GN Name=LOC106576372 {ECO:0000313|RefSeq:XP_014008981.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014008981.1};
RN [1] {ECO:0000313|RefSeq:XP_014008981.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014008981.1};
RG RefSeq;
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 RefSeq; XP_014008981.1; XM_014153506.1.
DR AlphaFoldDB; A0A1S3N1T9; -.
DR GeneID; 106576372; -.
DR OrthoDB; 9421at2759; -.
DR Proteomes; UP000087266; Chromosome ssa17.
DR Bgee; ENSSSAG00000013774; Expressed in liver and 15 other cell types or tissues.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; 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 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_014008981.1};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transferase {ECO:0000313|RefSeq:XP_014008981.1}.
FT DOMAIN 10..281
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 437..496
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 164..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 496 AA; 56994 MW; 0F97A04AE529085F CRC64;
MSGSYDDSMV DVSSDSFWEV GNYKRTVRRV DDGSRLCNDL MNCLHERARI EKSYAQQLTE
WSKRWRQLIE KGPQYGTLER AWGALCTEAE KVSELHMEVK AALMGEDFEK LKVWQRDYYH
KQMIGGFKET KEADDGFRKA QKPWAKKLKE METMKKAYHG ACKEEKLATS RENNSKLENN
SNPEAQKKLQ DKVEKCQQEM EKTKERYEKS LEELDKVTPQ YMENMEQVFE QWQQFEDKRI
TFFKALLLEV KHHLDLSTNH KFQTVYHTLE DTISAADAEE DLKWFRSNHG PGMPMNWPQF
EDWSIDLNRT LSRRETKKKP SDGVTLTGIS QMEEQQAAKS SSSLTVPTST ETVGSNPFED
DDDEDLQGTV KEQPTVVVNN NNNSSPLNVK KVEEVKTSSS VEKSQEWSDE ETGVNPFSIE
DANGDGNPFE VEPASSGVSV AVRALYDYEG QEQDELSFKA GEEFTKIGNE DDQGWCRGRL
KDGVVGLYPA NYVDDI
//