ID A0A1S3P8L7_SALSA Unreviewed; 848 AA.
AC A0A1S3P8L7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Cas scaffolding protein family member 4-like isoform X2 {ECO:0000313|RefSeq:XP_014023919.1, ECO:0000313|RefSeq:XP_014023929.1};
GN Name=LOC106583834 {ECO:0000313|RefSeq:XP_014023919.1};
GN Synonyms=LOC106583838 {ECO:0000313|RefSeq:XP_014023929.1};
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_014023919.1};
RN [1] {ECO:0000313|RefSeq:XP_014023919.1, ECO:0000313|RefSeq:XP_014023929.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014023919.1,
RC ECO:0000313|RefSeq:XP_014023929.1};
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_014023919.1; XM_014168444.1.
DR RefSeq; XP_014023929.1; XM_014168454.1.
DR GeneID; 106583834; -.
DR CTD; 57091; -.
DR OrthoDB; 2902504at2759; -.
DR Proteomes; UP000087266; Chromosome ssa22.
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; cd11844; SH3_CAS; 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; 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; CAS SCAFFOLDING PROTEIN; 1.
DR PANTHER; PTHR10654:SF19; CAS SCAFFOLDING PROTEIN FAMILY MEMBER 4; 1.
DR Pfam; PF12026; CAS_C; 1.
DR Pfam; PF08824; Serine_rich; 1.
DR Pfam; PF14604; SH3_9; 1.
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 1..63
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 67..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..298
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..711
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 848 AA; 92660 MW; 64A6A21FE578D258 CRC64;
METLLAKALY DNIAECSDEL GFRKGDVVTV LQQEVEESCG WWMCFLSGRQ GLAPANRLQL
LPQTPAQTQG KVTGPHAGCV DPGSSHDSDS DRPGNLYQIP SISRPTQSSS PTYECMDRVY
KASVSSMFSG CSKGEVYDVP SLVRRASIFP VYAVPPPGVP DPSYDIPIPS SVPSSGGYDT
SPSPRRQPSS YSTLPNPRKS DWIYDVPSSS EKPGGEPGYY THLPSGGEPG YYTTLTSKAL
SSDGQLHDTL TNDRNCSGQG RGSAQSFYDI PKPRSPPQGS KDPHNPPRVL PRPPLYDRPP
GQRQTDKEHC VYAVPPREQL SVSVPHRGHH VPLECRGDSG PTYDHPNAQG RLQRGRLGLV
AEALETRPGK GGTLLQEGDE ERGRTTTSTS DKQRISTAST SSTSSSCDSL ALCSSSSPEP
QREVCLSQEE ACRRLLLLQQ EVCREVPRLM EFVSSSWRSR DHLEKHLTEI RSAAEGVAGS
VTSFLTFALD VKGNARRLTD SNLQARLQRQ LSVLEDSGLI LQQAVSSLGV AGWPLPLLAQ
DPAQNHTPDQ LDSLVRVTRT IPEDVKRMVS IVNANAKLLF RPSTSTSTTN NTSTSTSQFV
KKRTEQGEES GANHHDNTQL QEDQKRCVSE PQVCVDGSRR SSEPLSPRKP SMSDSGDTPR
RTSEPQVSPS ARMASQSEPQ VSPSARMASQ SEPQVSPSPG KSFNSRVDST KRQPTLSEHC
RLYFGAMQKA IGVFITSLDS QTPEKFISHS KLVIMVGQRL VDTLYREAQK GESQRREPGS
VSESKLGPSQ SQVLLCKCNN MCALLKQLAV ATKKAALHYP EKQALQEAQD FAKELAQRAQ
HFRISLDL
//
