ID A0A1S3KLS0_SALSA Unreviewed; 940 AA.
AC A0A1S3KLS0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Breast cancer anti-estrogen resistance protein 1-like isoform X1 {ECO:0000313|RefSeq:XP_013979671.1};
GN Name=LOC106560839 {ECO:0000313|RefSeq:XP_013979671.1};
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_013979671.1};
RN [1] {ECO:0000313|RefSeq:XP_013979671.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013979671.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000256|ARBA:ARBA00004246}.
CC -!- SIMILARITY: Belongs to the CAS family. {ECO:0000256|ARBA:ARBA00007848}.
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DR RefSeq; XP_013979671.1; XM_014124196.1.
DR AlphaFoldDB; A0A1S3KLS0; -.
DR GeneID; 106560839; -.
DR KEGG; sasa:106560839; -.
DR OrthoDB; 2902504at2759; -.
DR Proteomes; UP000087266; Chromosome ssa10.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd11552; Serine_rich_BCAR1; 1.
DR CDD; cd12001; SH3_BCAR1; 1.
DR Gene3D; 1.20.120.230; Alpha-catenin/vinculin-like; 1.
DR Gene3D; 1.20.120.830; Serine-rich domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR035745; BCAR1_SH3.
DR InterPro; IPR021901; CAS_C.
DR InterPro; IPR037362; CAS_fam.
DR InterPro; IPR014928; Serine_rich_dom.
DR InterPro; IPR038319; Serine_rich_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR10654:SF15; BREAST CANCER ANTI-ESTROGEN RESISTANCE PROTEIN 1; 1.
DR PANTHER; PTHR10654; CAS SCAFFOLDING PROTEIN; 1.
DR Pfam; PF12026; CAS_C; 1.
DR Pfam; PF08824; Serine_rich; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR PRINTS; PR01887; SPECTRNALPHA.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 18..80
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 86..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 940 AA; 103584 MW; 8875CB4AF10F4AA8 CRC64;
MSVPVFCRMF DCLQRASSEN VLAKALYDNV AESPDELSFR KGDIMTVLER DTQGLDGWWL
CSLHGRQGIV PGNRLKILVG MYDKAGQQQQ PPPLQASQAG SAQTQSPSQL AFPPQSAYTK
PSPSSQYTAM HPAFSNPGPV PALPDSIYMM PPNHGKPSPS SLYQIPTGPQ APPKAPMLAQ
KQYHAPVQDI YQVPPSMGPA PVQDIYQVPP SARGPVPGQD IYQVPPSLNQ TQIPPSIEKR
SWDSKPLGKV VVPTRVGQVY VYDTGKSEQD EYDVPPRHMP PSQQSQDIYD VPPTRAQYSQ
QVYDTPPMAV KGPPSGQDIY DTPPSVDKSQ LLSQQTVYDF PPSVSKDVPD TPIREETYDV
PPHFAKLKSL ESQNQGYLIP GGPEPPIPED VYNIPPPPLT GKHHPDAPLG QEIYDIPASL
RKGGPHDPQD VYDFPRERPA GEDSIYDIPP QVVRDAGATE ELTVSFKRLS ASSTGSTRSN
LSTSSLDMVP VRELAVPGQA GPGKLLILDL DQAMERLSRL QQGVEGSVSL LMSFISGNWR
SPTQMEANLP AIRQAVDRMR VAVRDLLEFA RGAVANSAQA TDRTLQAKLG KQVQKMEEAF
QGLVKSSQAL DAVAWAPSAL MTPSAGSSGD DLDRLVMCAR GVPDDTKQLA SFLHGNASLL
FKRTNKQQQL PLPPVPHTAD LMGQMTNNNI SAYQMGDGRA NIQSRPLPSP PKLTAEEETR
DRPYETTEEG WMEDYDYVHL QGKEEFEKNQ RQLLEKGTRH NKTTLEQQQQ LKQFERLEQE
VSRPINNDIS GWTPPPHYPT AQRSKLSMGD RQLLLFYSEQ CESNVTTLTN AIDAFYSSIN
NNQPPKIFVA HSKFVILSAH KLVFIGDTLS RQAKSPEVRA HVAQHSNTLC DKLKDIVVST
KTAALQYPSP GAARDMTERV RELAGCTQQF RMALGQLVAM
//