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Database: UniProt
Entry: A0A1S3N1T9_SALSA
LinkDB: A0A1S3N1T9_SALSA
Original site: A0A1S3N1T9_SALSA 
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
//
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