ID A0A3B4CUF3_PYGNA Unreviewed; 771 AA.
AC A0A3B4CUF3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Cas scaffold protein family member 4 {ECO:0000313|Ensembl:ENSPNAP00000014154.1};
OS Pygocentrus nattereri (Red-bellied piranha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Pygocentrus.
OX NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000014154.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000014154.1}
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; A0A3B4CUF3; -.
DR STRING; 42514.ENSPNAP00000014154; -.
DR Ensembl; ENSPNAT00000021993.1; ENSPNAP00000014154.1; ENSPNAG00000020098.1.
DR GeneTree; ENSGT00950000183008; -.
DR OMA; TYERMDM; -.
DR Proteomes; UP000261440; 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 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 290..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..620
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 771 AA; 85809 MW; 0EF58CF319A15CA8 CRC64;
MNTLFAKALY DNTAESLDEL AFHKGDIVTV MEQNVEGSTG WWKCSLHGKE GLAPANRLMR
LSQAEAEALG LRSQSIYQIP KVPQPLEASP TYEIMERFYK VPSMQATQVT TPFPQKHKTP
EVPEGTISPH RVDVYDVPNL ARNGSIPKFE RTCVFQVYAV PPSIPQEPNY DIPVPSNSEA
HQRVACGYST MPNLRKSEWI YDVPVAPEKS RGEAVNYGTI PSKCTNSSKQ LYDTLPARVW
PATSASSLYD IPKSSMAAQQ SVDSSKPGNE GIYDVPPAAK QRETPLEVLP LQKQQNLNLN
DSDKGPVPLE YRGNSRPMYD FPRGRPSWGR KAEMSNQSQE GAISVESEES VEKGRGLSVP
KNQRSSTAST SSTTSSSSRS SCDSLMLSSP SPELLREITA PQEEVSQKLL DLQEVVCKAI
PKLMDFVSSS WRCREHLGQH LQEIRIAAED VANSINSFLD FALDVRGNAR RLTDSNLQAR
LQKQLSIVED SGLILQQSVE DLGGLGWSLD ALVQDPEKPH TPDQLERFVM VARTVPEDVK
RLVSILNANG KLLFRSSSKE PESSKSTSPA DRTTSLGRNE PLPDSEGDDN DYVQLQTKTE
FEQQQQIKEK DDTNEGNKGK QVNDFLRKYT SQSNFCLEYE QTSSTRDVCP SKSQISDHCR
LYFGAIKKAI TVFVVSLEEG QPPEKFIAHG KLVIMVGQRL MDSLCSEAQS RPDCQELLCK
SNHLCALLKQ LAVATKKAAM HFPDKVAIQE ARDFAKELAQ RAHHFRMSLD L
//
