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CASS4_PIG
ID   CASS4_PIG               Reviewed;         784 AA.
AC   A5GFW5; A5GFW4;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Cas scaffolding protein family member 4 {ECO:0000250|UniProtKB:Q9NQ75};
GN   Name=CASS4 {ECO:0000250|UniProtKB:Q9NQ75};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1] {ECO:0000312|EMBL:CAN13139.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Porcine genome sequencing project;
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Docking protein that plays a role in tyrosine kinase-based
CC       signaling related to cell adhesion and cell spreading. Regulates
CC       PTK2/FAK1 activity, focal adhesion integrity, and cell spreading (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts (via SH3 domain) with PTK2/FAK1 (via C-terminus).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:Q9NQ75}. Cell junction, focal adhesion
CC       {ECO:0000250|UniProtKB:Q9NQ75}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=A5GFW5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A5GFW5-2; Sequence=VSP_052952;
CC   -!- DOMAIN: The SH3 domain interacts with the C-terminal region of
CC       PTK2/FAK1. {ECO:0000250}.
CC   -!- PTM: Phosphorylated on tyrosines by SRC.
CC       {ECO:0000250|UniProtKB:Q9NQ75}.
CC   -!- SIMILARITY: Belongs to the CAS family. {ECO:0000255}.
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DR   EMBL; CR956640; CAN13138.1; -; Genomic_DNA.
DR   EMBL; CR956640; CAN13139.1; -; Genomic_DNA.
DR   RefSeq; NP_001103901.2; NM_001110431.2. [A5GFW5-1]
DR   AlphaFoldDB; A5GFW5; -.
DR   SMR; A5GFW5; -.
DR   STRING; 9823.ENSSSCP00000007986; -.
DR   PaxDb; A5GFW5; -.
DR   PRIDE; A5GFW5; -.
DR   Ensembl; ENSSSCT00000088123; ENSSSCP00000062821; ENSSSCG00000007495. [A5GFW5-2]
DR   Ensembl; ENSSSCT00025104952; ENSSSCP00025046772; ENSSSCG00025075922. [A5GFW5-2]
DR   Ensembl; ENSSSCT00045033914; ENSSSCP00045023512; ENSSSCG00045019865. [A5GFW5-1]
DR   Ensembl; ENSSSCT00050058992; ENSSSCP00050025312; ENSSSCG00050043342. [A5GFW5-1]
DR   Ensembl; ENSSSCT00070036671; ENSSSCP00070030660; ENSSSCG00070018591. [A5GFW5-1]
DR   Ensembl; ENSSSCT00070036674; ENSSSCP00070030663; ENSSSCG00070018591. [A5GFW5-2]
DR   GeneID; 100126293; -.
DR   KEGG; ssc:100126293; -.
DR   CTD; 57091; -.
DR   eggNOG; ENOG502QUJM; Eukaryota.
DR   GeneTree; ENSGT00950000183008; -.
DR   HOGENOM; CLU_820243_0_0_1; -.
DR   InParanoid; A5GFW5; -.
DR   TreeFam; TF328782; -.
DR   Proteomes; UP000008227; Chromosome 17.
DR   Proteomes; UP000314985; Chromosome 17.
DR   Bgee; ENSSSCG00000007495; Expressed in blood and 23 other tissues.
DR   ExpressionAtlas; A5GFW5; baseline.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR   GO; GO:0090527; P:actin filament reorganization; IBA:GO_Central.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR   GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; ISS:UniProtKB.
DR   GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISS:UniProtKB.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR   CDD; cd12000; SH3_CASS4; 1.
DR   Gene3D; 1.20.120.830; -; 1.
DR   InterPro; IPR021901; CAS_C.
DR   InterPro; IPR037362; CAS_fam.
DR   InterPro; IPR035512; CASS4.
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; PTHR10654; 1.
DR   PANTHER; PTHR10654:SF19; PTHR10654:SF19; 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; SSF50044; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   3: Inferred from homology;
KW   Alternative splicing; Cell adhesion; Cell junction; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Phosphoprotein; Reference proteome; SH3 domain.
FT   CHAIN           1..784
FT                   /note="Cas scaffolding protein family member 4"
FT                   /id="PRO_0000351206"
FT   DOMAIN          11..73
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          343..376
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          614..635
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          466..536
FT                   /evidence="ECO:0000255"
FT   MOD_RES         197
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NQ75"
FT   MOD_RES         246
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NQ75"
FT   MOD_RES         302
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NQ75"
FT   MOD_RES         373
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NQ75"
FT   MOD_RES         387
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NQ75"
FT   VAR_SEQ         212..648
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_052952"
SQ   SEQUENCE   784 AA;  86279 MW;  FD6AA235216F37A9 CRC64;
     MKGAGGPDGA PKALLARALY DNHPDCSDEL AFCRGDILTI LEQDVPESEG WWTCLLHGRQ
     GLAPANRLQI LEEAPADGPC PPFFGGLEEA PGRSQENYEV PSPPTPGPVY EQMKSWVEGP
     PPPTVQIYEF PDPPTCARIV CEKTLSFPKQ AIFTIPRAAR TSLPALPCQV YDVPAQSRCP
     PASKEPGKQQ LYDIPPSRQK ATLGPLSSQA NGQNVPLTSA TALRRGGCNT LPNPQKSEWI
     YDTPVSLEKA GVQKASLANS GEELGHRGLP RYMSSFHSPP NSIARSHPPH PQKNGPMQKK
     LSLPEIPCYS FPPPKCMFPL DESVSYKVPS SFLIPRVEQQ NTTPNIYDVP RAMPDVPQAG
     KELGKAGGPS ENSVDHSSSW FCSRAASLSP EPDSISVSSS DSRASVLSSC SSTSTDSSSS
     SFSEEAAKEL PLDLDSAKET VTALQHKVAS SVSSLMHFVS RKWRFRDSLE ANIDAIRRAT
     DRIEESLREF LDFAHGVRGT AGNLTDSNLQ TKIRDQLQTI ANAYQILLET KERLESCGWS
     LEVLATDKVQ NSPDDLERFV LVARTVPEDI KRFASIVIAN GRLLFKSNCE KEEPVQWTPN
     AEFKLARRIQ LPQKEGESYQ RKAPFQKQRA SEQPPELIEK NKTNACGQNP GSLIPRPLSQ
     QNPEKRIHLS EHCRLYFGAL LKAIGVLNGS LSNRQPPETF ITQSKLIIMV GQKLVDTLCK
     ETQERDFRNE ILCGSSHLCS LLRNLALATK HAVLEYPSPA ALGHLQAEAR KLEQHTQQFR
     GTLE
 
 
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