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PDS5A_DANRE
ID   PDS5A_DANRE             Reviewed;        1320 AA.
AC   A1L1F4;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Sister chromatid cohesion protein PDS5 homolog A;
GN   Name=pds5a {ECO:0000250|UniProtKB:Q29RF7}; ORFNames=zgc:66331;
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] {ECO:0000312|EMBL:AAI29036.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May regulate sister chromatid cohesion during mitosis and
CC       couple it to DNA replication. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with the cohesin complex. Binds chromatin in a
CC       cohesin-dependent manner (By similarity).
CC       {ECO:0000250|UniProtKB:Q29RF7}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q29RF7}.
CC   -!- SIMILARITY: Belongs to the PDS5 family. {ECO:0000305}.
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DR   EMBL; BC129035; AAI29036.1; -; mRNA.
DR   RefSeq; NP_957286.2; NM_200992.2.
DR   AlphaFoldDB; A1L1F4; -.
DR   SMR; A1L1F4; -.
DR   STRING; 7955.ENSDARP00000109877; -.
DR   PaxDb; A1L1F4; -.
DR   PeptideAtlas; A1L1F4; -.
DR   PRIDE; A1L1F4; -.
DR   GeneID; 393967; -.
DR   KEGG; dre:393967; -.
DR   CTD; 23244; -.
DR   ZFIN; ZDB-GENE-040426-1612; pds5a.
DR   eggNOG; KOG1525; Eukaryota.
DR   InParanoid; A1L1F4; -.
DR   OrthoDB; 69768at2759; -.
DR   PhylomeDB; A1L1F4; -.
DR   Reactome; R-DRE-2467813; Separation of Sister Chromatids.
DR   Reactome; R-DRE-2468052; Establishment of Sister Chromatid Cohesion.
DR   Reactome; R-DRE-2470946; Cohesin Loading onto Chromatin.
DR   Reactome; R-DRE-2500257; Resolution of Sister Chromatid Cohesion.
DR   PRO; PR:A1L1F4; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   GO; GO:0007064; P:mitotic sister chromatid cohesion; IBA:GO_Central.
DR   GO; GO:0008156; P:negative regulation of DNA replication; ISS:UniProtKB.
DR   Gene3D; 1.25.10.10; -; 2.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR039776; Pds5.
DR   PANTHER; PTHR12663; PTHR12663; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Mitosis; Nucleus; Reference proteome; Repeat.
FT   CHAIN           1..1320
FT                   /note="Sister chromatid cohesion protein PDS5 homolog A"
FT                   /id="PRO_0000296345"
FT   REPEAT          156..195
FT                   /note="HEAT 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          272..310
FT                   /note="HEAT 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          388..426
FT                   /note="HEAT 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          709..747
FT                   /note="HEAT 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          990..1028
FT                   /note="HEAT 5"
FT                   /evidence="ECO:0000255"
FT   REGION          1158..1320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1158..1184
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1224..1240
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1281..1296
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1297..1313
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1320 AA;  148958 MW;  B5FB528659C4129E CRC64;
     MEFPQQPQQQ RPAGDGKITY PLGVKEITDK ISNDEVVKRL KLVVKTYMDM DQDSEEEKQQ
     YLALALHLAS EFFLRNPNKD VRLLVACCLA DIFRIYAPEA PYTSHDKLKE IFLFITRQLK
     GLEDTKSPQF NRYFYLLENL AWVKSYNICF ELEDCNEIFI QLFKTLFSVI NNSHNQKVQM
     HMLDLMSSII MEGDGVTQEL LDTILINLIP AHKNLNKQAY DLARTLLKRT VQTIETCIAS
     FFNQVLVMGK SSVSDLSEHV FDLIQELFAI DPLLLVSVMP QLEFKLKSND GEERLAVVKL
     LAKLFGAKDS ELATQNRPLW QCFLGRFNDI HVPVRLECVK FASHCLMNHP DLAKDLTEFL
     KVRSHDPEEA IRHDVIVTII NAGKKDLNLV NDQLLGFVRE RMLDKRWRVR KEAMMGLAQL
     FKKYCLHHEA GKESALKISW IKDKLLHIYY QNSIDDKLLV EKIFAQYMVP HSLETEEKMK
     CLYYLYACLD TNAVKALNEM WKCQNMLRGL VRELLDLHKL PTSEANTSAM FGKLMTIAKN
     LPDPGKAQDF MKKFNQVLGE DEKLRLQLEQ LISPTCSCKQ AEQCVREITR KLTFPKQPTN
     PFLEMVKFLL ERIAPVHIDS EAISALVKLL NKSIEGTADD EDEGVTPDTA IRAGLELLKV
     LSFTHPTAFH SAETYESLLQ CLKMEDDKVA EAAIQIFRNT GQKIETELPQ IRSTLIPILH
     QKAKRGTPHQ AKQAVHCIHA IFHNKEVQLA QIFEPLSRSL NADVPEQLIT PLVSLGHISM
     LAPDQFASPM KSIVANFIVK DLLMNDRSVG NKNGRLWTAD DEVSPEVLAK VQAIKLLVRW
     LLGMKNNQSK SANSTLRLPS AMLVSEGDLT EQKKISKSDM SRLRLAAGSA ILKLAQEPCY
     HDIITPEQFQ LCGLVINDEC YQVRQIYAQK LHVALVKLLL PLEYMAVFAL CAKDPVKERR
     AHARQCLLKN ISVRREYIKQ NPMAHEKLLS LLPEYVVPYM IHLLAHDPDL TKPQDLEQLR
     DVKECLWFML EVLMTKNENN SHSFLRKMVE NIKQTKDAQC PDDPKANEKL YIVCDVALFV
     IANKSTSCHL DSPKDPVLPS KFYTPPDKEF VNDKEYLSAE AKIVLQTGKI QQPPKQTGVL
     GAVNKPLTVT ARRPYIKTFT SETGSNASTN SQPSSPATNK SRDVSSEVGA RENEENPVIT
     KAVSVKKEEA AQPSGRKRAA PASDGTENSV SSNPSAGSQP PLNKPRRGRP PKNSAGAATQ
     EKEAGATTGA GAGRGRKRAA PSQDPSSTAS TDALSDKTPK QQKEAEPKRA APQRQIDLQR
 
 
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