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Database: UniProt
Entry: F7G8D3_CALJA
LinkDB: F7G8D3_CALJA
Original site: F7G8D3_CALJA 
ID   F7G8D3_CALJA            Unreviewed;       781 AA.
AC   F7G8D3;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 3.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Cas scaffold protein family member 4 {ECO:0000313|Ensembl:ENSCJAP00000020795.4};
GN   Name=CASS4 {ECO:0000313|Ensembl:ENSCJAP00000020795.4};
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000020795.4, ECO:0000313|Proteomes:UP000008225};
RN   [1] {ECO:0000313|Ensembl:ENSCJAP00000020795.4}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCJAP00000020795.4}
RP   IDENTIFICATION.
RG   Ensembl;
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   AlphaFoldDB; F7G8D3; -.
DR   Ensembl; ENSCJAT00000021981.5; ENSCJAP00000020795.4; ENSCJAG00000011299.5.
DR   GeneTree; ENSGT00950000183008; -.
DR   Proteomes; UP000008225; Chromosome 5.
DR   Bgee; ENSCJAG00000011299; Expressed in ovary and 3 other cell types or tissues.
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; cd11551; Serine_rich_CASS4; 1.
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:UP000008225};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          11..73
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          202..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          263..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          369..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          612..662
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..246
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        638..661
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   781 AA;  86689 MW;  6F9B8B6F4E07646B CRC64;
     MKGTGVVDAV PKALLARALY DNCPDCSDEL AFNRGDILTI LEQQVPESEG WWKCLLHGRQ
     GLAPANRLQI LTEVAADRLR PPFLRGLEEA PASSEETYQV PTLPHPPTPG PVYEQMRSWV
     EGPQPPTAQV YEFPDPPTSA RIICEKTLSF PKQAILTLPR PARASLPTLP SQVYDVPTQH
     WGPGALKEPE KRQLYDIPAS PKKAGLHPPT GQASAQGVPQ LSPTTLRRGG YSTLPNPQKS
     EWIYDTPGKT SIRNMSLTSF AEESGPHIVP SSSSTFHNPP SGRARSLTPQ LNNRVLMQKK
     LSVPEIPSYG FLAPRDTFPL DTDVSYKVPS SFLMPRVEQQ NTKPNIYDIP KAMSSVFPAG
     KELTKINEVS ENSTGHDSSW FSRRTTSLSP EPKRLSVSSS DSRASVVSSC STTSTDSSSS
     SSSEESAKEL FLDLDVAKET VMALQHKVVS SVAGLMLFVS RKWRFRDYLE ANIDAIHRAT
     DHIEESVREF LDFAQGVHGT ACNLTGSHLQ NRIRDQMQTI SNSYRILLET KESLDNRHWP
     LEVLVTDNVQ NSPDDLERFV MVARMLPEDI KRFASIVIAN GRLLFKQNDE TVQLTPNAEF
     KCKKCIQPPQ RETESYQNST LSTKQREDEH SSELLKKNRA NICGQNPGSL LPQTLSQQTP
     EKKPHLSEHC RLYFGALFKA ISAFLSSLGS SQPPDILITQ SKLVIMVGQK LVDTLCKETQ
     ERDVRNEILH SSSHLCSLLK DVALATKNAV LQYPSPAALG HLQAEAEKLE QHTRQFRGTL
     G
//
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