ID   APC5_PONAB              Reviewed;         755 AA.
AC   Q5RE52;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Anaphase-promoting complex subunit 5;
DE            Short=APC5;
DE   AltName: Full=Cyclosome subunit 5;
GN   Name=ANAPC5;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the anaphase promoting complex/cyclosome
CC       (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls
CC       progression through mitosis and the G1 phase of the cell cycle. The
CC       APC/C complex acts by mediating ubiquitination and subsequent
CC       degradation of target proteins: it mainly mediates the formation of
CC       'Lys-11'-linked polyubiquitin chains and, to a lower extent, the
CC       formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By
CC       similarity). {ECO:0000250}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: The mammalian APC/C is composed at least of 14 distinct
CC       subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6,
CC       ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and
CC       ANAPC16 that assemble into a complex of at least 19 chains with a
CC       combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1
CC       and FBXO5. {ECO:0000250|UniProtKB:Q9UJX4}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UJX4}.
CC       Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9UJX4}.
CC   -!- SIMILARITY: Belongs to the APC5 family. {ECO:0000305}.
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DR   EMBL; CR857685; CAH89955.1; -; mRNA.
DR   RefSeq; NP_001124917.1; NM_001131445.1.
DR   AlphaFoldDB; Q5RE52; -.
DR   SMR; Q5RE52; -.
DR   STRING; 9601.ENSPPYP00000005751; -.
DR   Ensembl; ENSPPYT00000005971; ENSPPYP00000005751; ENSPPYG00000005048.
DR   GeneID; 100171787; -.
DR   KEGG; pon:100171787; -.
DR   CTD; 51433; -.
DR   eggNOG; KOG4322; Eukaryota.
DR   GeneTree; ENSGT00390000018674; -.
DR   HOGENOM; CLU_020635_0_0_1; -.
DR   InParanoid; Q5RE52; -.
DR   OMA; TVMHLTG; -.
DR   OrthoDB; 240631at2759; -.
DR   TreeFam; TF105444; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000001595; Chromosome 12.
DR   GO; GO:0005680; C:anaphase-promoting complex; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR   GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0070979; P:protein K11-linked ubiquitination; ISS:UniProtKB.
DR   Gene3D; 1.25.40.10; -; 1.
DR   InterPro; IPR037679; Apc5.
DR   InterPro; IPR026000; Apc5_dom.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR12830; PTHR12830; 1.
DR   Pfam; PF12862; ANAPC5; 2.
DR   SMART; SM00028; TPR; 4.
DR   SUPFAM; SSF48452; SSF48452; 2.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Mitosis; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; TPR repeat;
KW   Ubl conjugation pathway.
FT   CHAIN           1..755
FT                   /note="Anaphase-promoting complex subunit 5"
FT                   /id="PRO_0000307376"
FT   REPEAT          209..249
FT                   /note="TPR 1"
FT   REPEAT          250..300
FT                   /note="TPR 2"
FT   REPEAT          301..337
FT                   /note="TPR 3"
FT   REPEAT          338..378
FT                   /note="TPR 4"
FT   REPEAT          379..418
FT                   /note="TPR 5"
FT   REPEAT          419..466
FT                   /note="TPR 6"
FT   REPEAT          467..500
FT                   /note="TPR 7"
FT   REPEAT          501..540
FT                   /note="TPR 8"
FT   REPEAT          541..580
FT                   /note="TPR 9"
FT   REPEAT          581..620
FT                   /note="TPR 10"
FT   REPEAT          621..660
FT                   /note="TPR 11"
FT   REPEAT          661..696
FT                   /note="TPR 12"
FT   REPEAT          697..736
FT                   /note="TPR 13"
FT   MOD_RES         195
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJX4"
FT   MOD_RES         232
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJX4"
SQ   SEQUENCE   755 AA;  85077 MW;  174F68EAB44760EB CRC64;
     MASVHESLYF NPMMTNGVVH ANVFGIKDWV TPYKIAVLVL LNEMSRTGEG AVSLMERRRL
     NQLLLPLLQG PDITLSKLYK LIEESCPQLA NSVQIRIKLM AEGELKDMEQ FFDDLSDSFS
     GTEPEVHKTS VVGLFLRHMI LAYSKLSFSQ VFKLYTALQQ YFQNGEKKTV EDADMELTSR
     DEGERKMEKE ELDVSVREEE VSCSGPLSQK QAEFFLSQQA SLLKNDETKA LTPASLQKEL
     NNLLKFNPDF AEAHYLSYLN NLRVQDVFSS THSLLHYFDR LILTGAESKS NGEEGYGRSL
     RYAALNLAAL HCRFGHYQQA ELALQEAIRI AQESNDHVCL QHCLSWLYVL GQKRSDSYVL
     LEHSVKKAVH FGLPYLASLG IQSLVQQRAF AGKTANKLMD ALKDSDLLHW KHSLSELIDI
     SIAQKTAIWR LYGRSTMALQ QAQMLLSMNS LEAVNAGVQQ NNTESFAVAL CHLAELHAEQ
     GCFAAASEVL KHLKERFPPN SQHAQLWMLC DQKIQFDRAM NDGKYHLADS LVTGITALNS
     IEGVYRKAVV LQAQNQMSEA HKLLQKLLVH CQKLKNTEMV ISVLLSVAEL YWRSSSPTIA
     LPMLLQALAL SKEYRLQYLA SETVLNLAFA QLILGIPEQA LSLLHMAIEP ILADGAILDK
     GRAMFLVAKC QVASAASYDQ PKKAEALEAA IENLNEAKNY FAKVDCKERI RDVVYFQARL
     YHTLGKTQER NRCAMLFRQL HQELPSHGVP LINHL