位置:首页 > 蛋白库 > ABP1_SACEX
ABP1_SACEX
ID   ABP1_SACEX              Reviewed;         617 AA.
AC   P38479;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Actin-binding protein;
GN   Name=ABP1;
OS   Saccharomyces exiguus (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX   NCBI_TaxID=34358;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CBS 379;
RX   PubMed=8110838; DOI=10.1016/0167-4781(94)90039-6;
RA   Lange U., Steiner S., Grolig F., Wagner G., Philippsen P.;
RT   "Cloning and sequencing of a gene coding for an actin binding protein of
RT   Saccharomyces exiguus.";
RL   Biochim. Biophys. Acta 1217:214-218(1994).
CC   -!- FUNCTION: May be involved in the spatial organization of cell surface
CC       growth. An overproduction of ABP1 causes the assembly of the cortical
CC       actin skeleton at inappropriate sites on the cell surface, resulting in
CC       delocalized surface growth (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Note=Cortical
CC       cytoskeleton.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X73977; CAA52156.1; -; Genomic_DNA.
DR   PIR; S42719; S42719.
DR   AlphaFoldDB; P38479; -.
DR   SMR; P38479; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   CDD; cd11961; SH3_Abp1_fungi_C2; 1.
DR   Gene3D; 3.40.20.10; -; 1.
DR   InterPro; IPR035718; Abp1_fungi_SH3_C2.
DR   InterPro; IPR002108; ADF-H.
DR   InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF00241; Cofilin_ADF; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00102; ADF; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SSF50044; 1.
DR   PROSITE; PS51263; ADF_H; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   3: Inferred from homology;
KW   Actin-binding; Cytoplasm; Cytoskeleton; Repeat; SH3 domain.
FT   CHAIN           1..617
FT                   /note="Actin-binding protein"
FT                   /id="PRO_0000064428"
FT   DOMAIN          7..136
FT                   /note="ADF-H"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT   REPEAT          202..211
FT                   /note="1-1"
FT   REPEAT          444..453
FT                   /note="1-2"
FT   REPEAT          495..510
FT                   /note="2-1"
FT   REPEAT          523..538
FT                   /note="2-2"
FT   DOMAIN          557..617
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REPEAT          591..600
FT                   /note="1-3"
FT   REGION          169..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          202..600
FT                   /note="3 X 10 AA approximate repeats"
FT   REGION          325..574
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          495..538
FT                   /note="2 X 16 AA repeats of E(7)-A-P-A-P-S-L-P-S-R"
FT   COMPBIAS        170..184
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        326..340
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        341..378
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        392..420
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        458..481
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        484..502
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        536..551
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   617 AA;  68420 MW;  540A785191B65F85 CRC64;
     MALEPIDATT HSRDIEQEYQ KVVRGTDNDT TWLIISPNTQ KEYLPSSTGS SFSDFLQSFD
     ETKVEYGIAR VSPPGSDVGK IILVGWCPDS APMKTRASFA ANFGTIANSV LPGYHIQVTA
     RDEDDLDEEE LLTKISNAAG ARYSIQAAGN SVPTSSASGS APVKKVFTPS LAKKESEPKK
     SFVPPPVREE PVPVNVVKDN DADDWDEPEI KERNFETNPL SDNKPAYEPI GKIDLKKVIA
     EETAKEDPRL INRIDPSADI AHLKQESKIH RDNDLDNLLK QEKTSSPAVG GTKPPLVNLI
     FVEMIIVIRL YKVSRPEKSP AQLWAEKKMK QNQQSDSAQE EQKPVETKTE IEIGVDNSDE
     MKIGDLKSRF EKLGAETETE PEPPVQWETD SIPTVVKPQT FGQPAANSKP ATQEVKKPFT
     PSNIGQRLPG MHTETPEHEE EDNDDDWGED EDEPPKRNIP PPVMPARESA PQQPLPPRNT
     EPEPVEEGEE EEEEEEEEEE EAPAPSLPSR NAAPEPEPEQ PQEEEEEEEA PAPSLPSRGS
     VPPPPPQRAV EPEEPAAEAP WATAEYDYEA GEDNELTFAE NDKIINIEFV DDDWWLGELE
     TTGQKGLFPS NYVVLGN
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024