ID A0A3B3RS42_9TELE Unreviewed; 713 AA.
AC A0A3B3RS42;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Cas scaffolding protein family member 4-like {ECO:0000313|Ensembl:ENSPKIP00000020556.1};
GN Name=CASS4 {ECO:0000313|Ensembl:ENSPKIP00000020556.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000020556.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000020556.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A3B3RS42; -.
DR STRING; 1676925.ENSPKIP00000020556; -.
DR Ensembl; ENSPKIT00000001174.1; ENSPKIP00000020556.1; ENSPKIG00000005288.1.
DR GeneTree; ENSGT00950000183008; -.
DR OrthoDB; 2902504at2759; -.
DR Proteomes; UP000261540; Unplaced.
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; PF00018; SH3_1; 1.
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 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 120..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 713 AA; 78747 MW; C0FF9730CD7E82FE CRC64;
MENLLAKALY DNTAESPEEL AFRKGDIITV MEQNVDGSHG WWRCSLHGRQ GLAPANRLHL
LSPAQMRAFA QVGLQTLCAG RSLTGSWSRP NIYQTPTVPR PPPSEAYEPM DRIYRVPFSP
KLNHESSGKR TTDLQTSMDK KHPSLKSEGK VSPSKIPGKC VAAAEVYDVP THPLRAFTTE
SNYDVPMSLA TENQQRTAIS GCTTLPNPRK SEWVYDVPLK PEKYHGTMMA KPRGQQDHMY
DTLPPRGALT LGASPAPQAY DVPNPSPCLK NRSTQRPEDQ ELIYDVPPTL KRQGIAQKSR
APAPVKPTGD VKELQPTQDD GDQQDGRPGS DISVSSTGSC ESSTPRSSSP ELVREVTLTQ
DEAACRLAEL QEAVCQAVPR LMVFVSSRWR TKDHLAKHIR EIQAAAQGIA GAMAQFLDFV
LDVRGNANQL SDANLQLRLH RQLSIVKDSG LILQEAMATL AGVGWQLNTL VQDSAQAQTP
DQLERFVMVA RTIPEDVRHL VSILNANGKL LFRRSQKDHD KPAGCDQPET KNSQMGDKQI
SDSGGEDNDY VHLQTKMEFE KQQMMEQKNK KSKQVAVNRP VAAVSPHALS EHCRLYFGAL
QKAIGVLVHS LQDGQPPESF IDQGKLVIMV GQRLVDTLCR EAQGQSAGTS QDLLYKGNQL
CALLKQLAVA TKKAALHYPD KTALQEVEDF AKELAHRAQH FRTLLDQSAV SRE
//
