ID A0A1V4KE49_PATFA Unreviewed; 831 AA.
AC A0A1V4KE49;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Cas scaffolding protein family member 4 isoform B {ECO:0000313|EMBL:OPJ82722.1};
GN Name=CASS4 {ECO:0000313|EMBL:OPJ82722.1};
GN ORFNames=AV530_004841 {ECO:0000313|EMBL:OPJ82722.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ82722.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ82722.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ82722.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ82722.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000256|ARBA:ARBA00004246}.
CC -!- SIMILARITY: Belongs to the CAS family. {ECO:0000256|ARBA:ARBA00007848}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OPJ82722.1}.
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DR EMBL; LSYS01003456; OPJ82722.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4KE49; -.
DR Proteomes; UP000190648; Unassembled WGS sequence.
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; cd11568; FAT-like_CASS4_C; 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 PRINTS; PR00452; SH3DOMAIN.
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:UP000190648};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 3..65
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 65..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 831 AA; 92278 MW; 78F10FC2890B7456 CRC64;
MKVNNALAKA LYDNKAECSD ELAFRKGDIL TVLDQNVIGS EGWWKCSLHG RQGLAPANRL
QLLAASPALP PPPSTRSSSA DSPSGQQNIY QVPSVPKPTT LSSTYEKMEG WIKSPARVPA
QGMYRVPALA AQLLSERTQS STSQHLFTLP RACRASVPNI RSEVYDVPSA QRREPSLTQS
GATPPSTRKR SVLVRPTECF QEEQKQLYNI PPSPEKAGAV LQKDSPASNL YDVPPKRESD
VSENESQKKL WGHYNTLPNP RKSEWIYDIP VSPEKTGLKQ NPSGHSSEKQ VLYDVPPTRY
KALTTNTEAK VVNPQLYDIP PTQRKLTLPD ICLYDVPPSR DILLLPQNSS CEVPSGLPAP
KAENLISEEN VYDIPKGLPT TVQSKKEMEK TSDSSGDPAH SAPSQLSRDA KLEQDRLSVS
SVDSKSSTLS TSSNSSAESF STSSSEEPVK EIKLDLGVAI ETLTRLQHSV SSSVASLMIF
VSSKWRLQEH LEKSIEEIHR AVDHVKVSLG EFLAFAQVVK VNAYYLTDNK LQTRIKKQLE
ILINSFKILT ETRGALNSCN WSLEALVLRK PQSNPDDLDR FVMVARTVPD DIKRFVSIII
ANGKLLFRKN EKEQEVKQSK VNPEYKVAKQ ITVPRRIEID SLQRNTPDKP NQSQVSSEKP
KENAPEDCDY VQLQAQKIIS ATEVAKKSKH SKPKVLPSAK KTVIQSKQES AKKIALSEQC
KLCFGALHKA IAVFTNSLSN NQPPEVFISH SKLIIMVGQK LVDSLCQETQ ERDARNDILH
GSSRFCGLLK NLALATKNAA IQYPNAGAMR ELQDQTEELS KYTQQFRAMM E
//
