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AB1IP_DANRE
ID   AB1IP_DANRE             Reviewed;         646 AA.
AC   Q6PFT9;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Amyloid beta A4 precursor protein-binding family B member 1-interacting protein;
DE   AltName: Full=APBB1-interacting protein 1;
GN   Name=apbb1ip;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Appears to function in the signal transduction from Ras
CC       activation to actin cytoskeletal remodeling.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm,
CC       cytoskeleton {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MRL family. {ECO:0000305}.
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DR   EMBL; BC057421; AAH57421.1; -; mRNA.
DR   RefSeq; NP_956928.1; NM_200634.1.
DR   AlphaFoldDB; Q6PFT9; -.
DR   SMR; Q6PFT9; -.
DR   STRING; 7955.ENSDARP00000117778; -.
DR   PaxDb; Q6PFT9; -.
DR   GeneID; 393607; -.
DR   KEGG; dre:393607; -.
DR   CTD; 54518; -.
DR   ZFIN; ZDB-GENE-040426-1318; apbb1ip.
DR   eggNOG; KOG3751; Eukaryota.
DR   InParanoid; Q6PFT9; -.
DR   OrthoDB; 786893at2759; -.
DR   PhylomeDB; Q6PFT9; -.
DR   Reactome; R-DRE-354192; Integrin signaling.
DR   Reactome; R-DRE-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
DR   Reactome; R-DRE-372708; p130Cas linkage to MAPK signaling for integrins.
DR   Reactome; R-DRE-5674135; MAP2K and MAPK activation.
DR   PRO; PR:Q6PFT9; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd01259; PH_APBB1IP; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR039664; GRB/APBB1IP.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR039665; PH_APBB1IP.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR000159; RA_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR11243; PTHR11243; 2.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00788; RA; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00314; RA; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50200; RA; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cytoplasm; Cytoskeleton; Membrane; Reference proteome.
FT   CHAIN           1..646
FT                   /note="Amyloid beta A4 precursor protein-binding family B
FT                   member 1-interacting protein"
FT                   /id="PRO_0000181350"
FT   DOMAIN          162..248
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT   DOMAIN          292..401
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   REGION          82..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          420..646
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..122
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        420..441
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        462..601
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   646 AA;  71002 MW;  A8CF0551E9932FA3 CRC64;
     MDDIDAMFSD MLQEMDLLTQ SLDAEVDSAP LAKPPTIPEP QEMNFSIGFA NFNESLNDLE
     DNDLDALMAD LVADISATEE KFATERDTSK GSVPVAPAPS KPQSNFSLPA SFDSSKPATS
     SNSIAAPPPP PAFKPSKEEE EEQLKADKIK LALEKLKEAK VKKLVVKVEI TDGSSKTLMV
     DERQTVRDVM DNLFEKTHCD CNVDWSVCET NPDLQTERAF EDHENLVEPL STWTRDTENK
     VLFQEKKHKY EVFKNPQIFY LWKKDKKSLK DMKEKDKEQL LEENFCGASV IVPDLEGVLY
     LKEDGKKSWK QRYFLLRASG LYYSPKGKTK ASRDLVCLVQ FDNVNVYYCK EYRIKYKAPT
     DHCFMLKHPQ IQKESQYIKF MCCDDEWSMN LWVTGIRVAK YGKQLYDNYK AAVRKASGSA
     SWANRTIQAS STASTPSPTP KAKAANGHAP QPPVENKVPS NQSSLPPPPP SMDFLPPPPP
     DPMFPPPPPA PPAPPAPPVP VSSTKVNKFP PPPKFPQSSF PPPPMDDLPP PPPPPEIADL
     PPDFLPPPPP SFVSHGGESL PPPPPDPVAS LPPPPPAFTS AGGAPPPPPP PPPPPAPAPA
     VNNPAGSVRK VAPPPPKRTT PQLAAPSGGD FMSELMNAMQ KKRTQP
 
 
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