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Database: UniProt
Entry: A0A2K5EX69_AOTNA
LinkDB: A0A2K5EX69_AOTNA
Original site: A0A2K5EX69_AOTNA 
ID   A0A2K5EX69_AOTNA        Unreviewed;       872 AA.
AC   A0A2K5EX69;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=SH3 domain-containing protein {ECO:0000259|PROSITE:PS50002};
OS   Aotus nancymaae (Ma's night monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC   Aotus.
OX   NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000037827.1, ECO:0000313|Proteomes:UP000233020};
RN   [1] {ECO:0000313|Ensembl:ENSANAP00000037827.1}
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; A0A2K5EX69; -.
DR   Ensembl; ENSANAT00000055911.1; ENSANAP00000037827.1; ENSANAG00000036378.1.
DR   GeneTree; ENSGT00950000183008; -.
DR   Proteomes; UP000233020; 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; cd11569; FAT-like_BCAR1_C; 1.
DR   CDD; cd12001; SH3_BCAR1; 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; IPR046976; BCAR1_C.
DR   InterPro; IPR035745; BCAR1_SH3.
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:SF15; BREAST CANCER ANTI-ESTROGEN RESISTANCE PROTEIN 1; 1.
DR   PANTHER; PTHR10654; CAS SCAFFOLDING PROTEIN; 1.
DR   Pfam; PF12026; CAS_C; 1.
DR   Pfam; PF08824; Serine_rich; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   PRINTS; PR01887; SPECTRNALPHA.
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:UP000233020};
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          67..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          373..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          399..451
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          610..660
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..92
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..158
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        429..447
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        626..655
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   872 AA;  93674 MW;  3C4063E6004E075C CRC64;
     MENVLAKALY DNVAESPDEL SFRKGDIMTV LEQDTQGLDG WWLCSLHGRQ GIVPGNRLKI
     LVGMYDKKPA GPGPGPPAAP AQPQPGLPQS LHAPAPPTSQ YTPMLPATYQ PQPDSVYLVP
     TPSKTPQGLY QAPGPSPQFQ SPPAKQTSTF SKQTPHHPFP SPATDLYQVP PGPGGPAQDI
     YQVPPSAGMG HDIYQVPPSM DTRSWEGTKP PAKVVVPTRV GQGYVYEAAQ PEQDEYDIPR
     HLLAPGPQDI YDVPPVRGLL PSQYGQEVYD TPPMAVKGPN GRAPLLEVYD VPPSVEKGLP
     LSSHHAVYDV PPSVSKDVPD GPLLREETYD VPPAFAKAKP FDPTRTPLVL ASPPLDSPPA
     EDVYDVPPPA PDLYDVPPGL RRPGPGTLYD VPRERVLPPE VADGGAADDG VYAVPPPAER
     EAPVDGKRLS ASSTGSTRSS QSASSLEVAG PGREPLELEV AVEALARLQQ GVSATVAHLL
     DLAGSTGGTR SWRSTPEPQE PLVQELRAAV AAVQSAVHEL LEFARSAVGN AAHTSDRALH
     AKLSRQLQKM EDVHQTLVAH GQALDTGRGG PGATPEDLDR LVACSRAVPE DAKQLASFLH
     GNASLLFRRT KAPAPGPEGG GTLHPNPTDK ASSIQSRPLP SPPKFTSQDS PDGQYENSEG
     GWMEDYDYVH LQGKEEFEKT QKELLEKGSI TRQGKSQLEL QQLKQFERLE QEVSRPIDHD
     LANWTPAQPL APGRTGSLGP SDRQLLLFYL EQCEANLTTL TNAVDAFFTA VATNQPPKIF
     VAHSKFVILS AHKLVFIGDT LSRQAKAADV RSQVTHYSNL LCDLLRGIVA TTKAAALQYP
     SPSAAQDMVE RVKELGHSTQ QFRRVLGQLA AA
//
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