ID A0A2K6CNX4_MACNE Unreviewed; 914 AA.
AC A0A2K6CNX4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=SH3 and PX domains 2B {ECO:0000313|Ensembl:ENSMNEP00000025391.1};
GN Name=SH3PXD2B {ECO:0000313|Ensembl:ENSMNEP00000025391.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000025391.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000025391.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the SH3PXD2 family.
CC {ECO:0000256|ARBA:ARBA00009628}.
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DR AlphaFoldDB; A0A2K6CNX4; -.
DR STRING; 9545.ENSMNEP00000025391; -.
DR Ensembl; ENSMNET00000049666.1; ENSMNEP00000025391.1; ENSMNEG00000036165.1.
DR GeneTree; ENSGT00940000158396; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000036165; Expressed in liver and 4 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0016176; F:superoxide-generating NADPH oxidase activator activity; IEA:InterPro.
DR GO; GO:0060348; P:bone development; IEA:Ensembl.
DR GO; GO:0022617; P:extracellular matrix disassembly; IEA:Ensembl.
DR GO; GO:0001654; P:eye development; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0072657; P:protein localization to membrane; IEA:Ensembl.
DR GO; GO:0006801; P:superoxide metabolic process; IEA:Ensembl.
DR CDD; cd06888; PX_FISH; 1.
DR CDD; cd12075; SH3_Tks4_1; 1.
DR CDD; cd12076; SH3_Tks4_2; 1.
DR CDD; cd12078; SH3_Tks4_3; 1.
DR CDD; cd12018; SH3_Tks4_4; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 4.
DR InterPro; IPR001655; P47PHOX.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR037961; SH3PXD2_PX.
DR InterPro; IPR035477; SH3PXD2B_SH3_1.
DR InterPro; IPR035478; SH3PXD2B_SH3_2.
DR InterPro; IPR035479; SH3PXD2B_SH3_3.
DR InterPro; IPR035480; SH3PXD2B_SH3_4.
DR PANTHER; PTHR15706:SF25; SH3 AND PX DOMAIN-CONTAINING PROTEIN 2B; 1.
DR PANTHER; PTHR15706; SH3 MULTIPLE DOMAIN; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF00018; SH3_1; 3.
DR Pfam; PF07653; SH3_2; 1.
DR PRINTS; PR00498; P47PHOX.
DR SMART; SM00312; PX; 1.
DR SMART; SM00326; SH3; 4.
DR SUPFAM; SSF64268; PX domain; 1.
DR SUPFAM; SSF50044; SH3-domain; 4.
DR PROSITE; PS50195; PX; 1.
DR PROSITE; PS50002; SH3; 4.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000233120};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 5..129
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 157..216
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 226..285
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 373..432
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 853..914
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 280..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..552
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..593
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..629
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..773
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 914 AA; 101716 MW; 7915F45BC4275FC4 CRC64;
MPPRRSIVEV KVLDVQKRRV PNKHYVYIIR VTWSSGSTEA IYRRYSKFFD LQMQMLDKFP
MEGGQKDPKQ RIIPFLPGKI LFRRSHIRDV AVKRLIPIDE YCKALIQLPP YISQCDEVLQ
FFETRPEDLN PPKDMVVARC HVCFLSTGGD QTSVDPMVLE QYVVVANYQK QESSEISLSV
GQVVDIIEKN ESGWWFVSTA EEQGWVPATC LEGQDGVQDE FSLQPEEEEK YTVIYPYTAR
DQDEMNLERG AVVEVIQKNL EGWWKIRYQG KEGWAPASYL KKNSGEPLPP KPGPGSPSHP
GALDLDGVSR QQNAVGREKE LLSSQRDGRF EGRPVPDGDT KQRSPKMRQR PPPRRDMTIP
RGLNLPKPPI PPQVEEEYYT IAEFQTTIPD GISFQAGLKV EVIEKNLSGW WYIQIEDKEG
WAPATFIDKY KKTSNASRPN FLAPLPHEVT QLRLGEAAAL ENNTGSEATG PSRPLPDAPH
GAMDSGLPWS KDWKGGKEVL RKASSDMSAS AGYEEISDPD MEEKPSLPPR KESIIKSEGE
LLERERQRTE QLRGPAPKPP CMILPMMPAK HTPPARDGRR PEPKPDKSKL FQLKNDMGLE
CGHKVLAKEV KKPNLRPISK SKTDLPEEKP DATPQNPFLK SRPQVRPKPT PSPKTEPPQG
EDQVDICNLR SKLRPAKSQD KSLLDGEGPQ AVGGQDVAFS RSFLPGEGSG RAQDRTGKQD
GLSPKEISCR APPRPAKTTD PVSKSVPVPL QEAPQQRPVV PPRRPPPPKK TCSSSRPLPE
VRGPQCEGHE SRAAPTPGRA LLVPPKAKPF LSNSLGGQDD TRGKGGLGPR GTGKIGENRE
EAAAAAVPSA DGLKDSLYVA VANFEGDKDT SSFQEGTVFE VREKNSSGWW FCQVLSGAPS
WEGWIPSNYL RKKP
//
