ID A0A2K5MT44_CERAT Unreviewed; 671 AA.
AC A0A2K5MT44;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Sorbin and SH3 domain containing 3 {ECO:0000313|Ensembl:ENSCATP00000028260.1};
GN Name=SORBS3 {ECO:0000313|Ensembl:ENSCATP00000028260.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000028260.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000028260.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR RefSeq; XP_011901182.1; XM_012045792.1.
DR AlphaFoldDB; A0A2K5MT44; -.
DR STRING; 9531.ENSCATP00000028260; -.
DR Ensembl; ENSCATT00000052511.1; ENSCATP00000028260.1; ENSCATG00000037430.1.
DR GeneID; 105579226; -.
DR CTD; 10174; -.
DR GeneTree; ENSGT00940000160558; -.
DR OMA; VHREPRL; -.
DR OrthoDB; 5407056at2759; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000037430; Expressed in spleen and 10 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0017166; F:vinculin binding; IEA:Ensembl.
DR GO; GO:0031589; P:cell-substrate adhesion; IEA:Ensembl.
DR GO; GO:0000165; P:MAPK cascade; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
DR CDD; cd11921; SH3_Vinexin_1; 1.
DR CDD; cd11924; SH3_Vinexin_2; 1.
DR CDD; cd11918; SH3_Vinexin_3; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR003127; SoHo_dom.
DR InterPro; IPR035609; Vinexin_SH3_1.
DR InterPro; IPR035608; Vinexin_SH3_2.
DR InterPro; IPR035607; Vinexin_SH3_3.
DR PANTHER; PTHR14167; SH3 DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR14167:SF54; VINEXIN; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF14604; SH3_9; 2.
DR Pfam; PF02208; Sorb; 1.
DR PRINTS; PR00499; P67PHOX.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 3.
DR SMART; SM00459; Sorb; 1.
DR SUPFAM; SSF50044; SH3-domain; 3.
DR PROSITE; PS50002; SH3; 3.
DR PROSITE; PS50831; SOHO; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 115..187
FT /note="SoHo"
FT /evidence="ECO:0000259|PROSITE:PS50831"
FT DOMAIN 380..439
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 454..515
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 612..671
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 82..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 671 AA; 75059 MW; 9283EF9737DF0267 CRC64;
MQGPPRSLPA GLSLDDFIPG HLQSHIGSSS RGTRVPVIRN GGSNTLNFQF HDPAPRTVCN
GCYTPRQDAS RHPDPTCYQT WPGPGSKPTA STKIPASQHA QNWSATWTKD SKRRDKRWVK
YEGIGPVDES GMPIAPRSSV DSPRDWYRRM FQQIHRKMPD LQLDWTFEEP PRDPRHLGAQ
QRPAHRPGPA ASSSGRSWDH SEELPRSTFS YRPGAFSTVL QPPNQVPRRR EKGDNVWTEE
SWNQFLQELE TGQRPKKPLV DDPGEKPSQP IEVLLERELA KLSAELDKDL RAIETRLPSP
KSSPAPRRAP EQRPPAGPAS AWSSSSPNAP YLGSARSLSP RRMADGGSPF LGRRDFVYPS
STRDPSASDG GISPARREEK KRKAARLKFD FQAQSPKELT LQKGDIVYIH KEVDKNWLEG
EHHGRLGIFP ANYVEVLPAD EIPKPIKPPT YQVLEYGEAV AQYTFKGDLE VELSFRKGEH
ICLIRKVNEN WYEGRITGTG RQGIFPASYV QVSREPRLRL CDDGPQLPAS PRLTAAARSA
HHPSSPSAPR SPADPTDWGG QTSPRRTGFS FSTQEPRPQT QNLGTPGPAL SHPRGPSHPL
DLGTSSTNAS QIHWTPYRAM YQYRPQNEDE LELREGDRVD VMQQCDDGWF VGVSRRTQKF
GTFPGNYVAP V
//
