ID A0A2Y9QCM7_DELLE Unreviewed; 807 AA.
AC A0A2Y9QCM7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Cas scaffolding protein family member 4 isoform X4 {ECO:0000313|RefSeq:XP_022453238.1};
GN Name=CASS4 {ECO:0000313|RefSeq:XP_022453238.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022453238.1};
RN [1] {ECO:0000313|RefSeq:XP_022453238.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022453238.1};
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_022453238.1; XM_022597530.2.
DR AlphaFoldDB; A0A2Y9QCM7; -.
DR Proteomes; UP000248483; 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; cd12000; SH3_CASS4; 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; IPR035744; CASS4_SH3.
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:UP000248483};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 5..67
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 273..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..668
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 807 AA; 89994 MW; A4754B2DDC67D91C CRC64;
MEKSVKMLLA RALYDNHPDC ADELAFCRGD ILTILEQNVP ESKGWWKCLL HGRQGLAPAN
RLEILVEAPA DRPCPPFLRG PEDAPTSSQE TYEVPTLLNP SSPGPVYEQM RSWVERPPPP
TVQVYEVPDP PASARIVCEK TLSFPKQALF TIPRPARTSL PALPCQVYDV PAQSRCLPAL
KEPGKQQQLY DILPSPQKAA LGPPASQPNG QSVPLMSSIA LRRGSCNTLP SPQKSEWIYD
TPVSPEKADV RNASLSSFVE KSGHRALPRY MSSFHSPQNS RARTLSPHPQ KNVPMQKKLS
LPEIPSHSFP PPRDAFPLDE GVSYKVPSSF LISRVEQKNT KLNIYDVPKA VLSVPQAGKE
LGKADGPSEN SMDHNSSWFS GRAASLSPEP DGLSVSSSDS RASVLSSCSS TSSHSSSSFS
EESAKELPLD LDLAKETVTA LQHKVDNSVA GLMLFVSRQW RFRDCLEANI HAIRRAADCI
EESLREFLDF ACGVRGTAWN LTDSKLQAKI RDQLQTISNS YQILLETKES LESCDWSLEV
LVTNKVQNSL DDLERFVLTA RMLPEDIKRF ASLVIANGRL LFKPNCEKED PMQLTPNAEF
KLAKSIWLPQ KEIESYQRNA SFQKQRESEH PPELLKKNRT DVCEQELPSL EEKEKPILEQ
RLDENKDLET QNPSSLSPRP LSQQNPEKKI RLSEHCRLYF GALFKAIGVL HSSLGNGQPP
EIFIAQSKLV IMVGQKLVDT LCQETQERDV RNEILRGSSH LCSLLKDLAL ATKHAVLQHP
SPAALQHLQA EAKKLEQHTQ QFRGMLE
//