ID W5N8C2_LEPOC Unreviewed; 786 AA.
AC W5N8C2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Amyloid beta (A4) precursor protein-binding, family A, member 2b {ECO:0000313|Ensembl:ENSLOCP00000016881.1};
GN Name=APBA2 {ECO:0000313|Ensembl:ENSLOCP00000016881.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000016881.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000016881.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AHAT01024861; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01024862; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01024863; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01024864; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5N8C2; -.
DR STRING; 7918.ENSLOCP00000016881; -.
DR Ensembl; ENSLOCT00000016911.1; ENSLOCP00000016881.1; ENSLOCG00000013693.1.
DR eggNOG; KOG3605; Eukaryota.
DR GeneTree; ENSGT00940000158943; -.
DR HOGENOM; CLU_013563_3_0_1; -.
DR InParanoid; W5N8C2; -.
DR OMA; MSPEHSG; -.
DR Proteomes; UP000018468; Linkage group LG3.
DR Bgee; ENSLOCG00000013693; Expressed in brain and 9 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0001540; F:amyloid-beta binding; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR CDD; cd00992; PDZ_signaling; 2.
DR CDD; cd01208; PTB_X11; 1.
DR Gene3D; 2.30.42.10; -; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR PANTHER; PTHR12345:SF12; AMYLOID-BETA A4 PRECURSOR PROTEIN-BINDING FAMILY A MEMBER 2; 1.
DR PANTHER; PTHR12345; SYNTENIN RELATED; 1.
DR Pfam; PF00595; PDZ; 2.
DR Pfam; PF00640; PID; 1.
DR SMART; SM00228; PDZ; 2.
DR SMART; SM00462; PTB; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 2.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50106; PDZ; 2.
DR PROSITE; PS01179; PID; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 402..542
FT /note="PID"
FT /evidence="ECO:0000259|PROSITE:PS01179"
FT DOMAIN 605..690
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 696..772
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..110
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..217
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 786 AA; 87158 MW; 1B084A3410103BAE CRC64;
MACNLPAMAH RKRQGTSSSM VEPRVRPCPA AFPAAPQRER RSDPEPEDLE NQPQRQFHPE
SPDLKDSRPA TPDHTDQDCQ DHSADGDSSS DYVNNTSEEE DYDEGLPEED EGVTYYIRYC
PEDDSYLEGM DCNDGDYIPH QEPSVETDEC QEAVEEWAES EGQCPSLDQD ADPQAYEDNP
EEVLNDRAAS LQTPLPGEEE EEEVEEEGEE SEEYCPNEEG FPQDYYSQEA NGNSVRVSPY
STRKADGEAG EDQEEDIDQI VAEIKMSMSM GSLSSGTDQS PEEPGNDSLP KDFKDVAAKA
DPVLYAGNRH EGRPKSLNIP AASRHSADVQ RGFKVRARTP EERQKWAQEQ VSNNPEQPRK
QQRSDLNGPA ENNNIPEQTK KTASFPSFVD VPGPCEPEDL IDGIIFAANY LGSTQLLSER
NPSKNIRMMQ AQEAVSRVKR VQKAAKIKKK VSPEGDPQTL TEVDLFISTQ RIKVLNADTQ
ETMMDNALRT ISYIADIGNI VVLMARRRMP RTASQDCIET TPGAQEGKKQ YKMICHVFES
EDVSTALVSQ WSGQSVEVLI MNESPSTEHN FQPSEFFRHS PCVHVHVQPR HMNLHWKSSS
DVWDFLQLEK QKGEILGVVI VESGWGSILP TVILANMMNG GPAARSGKLS IGDQIMSING
TSLVGLPLAT CQGIIKGLKN QTQVKLNIVS CPPVTTVLIK RPDLKYQLGF SVQNGIICSL
MRGGIAERGG VRVGHRIIEI NGQSVVATAH EKIVQALSNS VGEIHMKTMP AAMFRLLTGQ
ETPMYI
//
