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Database: UniProt
Entry: A0A2K6FDQ3_PROCO
LinkDB: A0A2K6FDQ3_PROCO
Original site: A0A2K6FDQ3_PROCO 
ID   A0A2K6FDQ3_PROCO        Unreviewed;      1998 AA.
AC   A0A2K6FDQ3;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Cytoskeleton associated protein 5 {ECO:0000313|Ensembl:ENSPCOP00000012088.1};
GN   Name=CKAP5 {ECO:0000313|Ensembl:ENSPCOP00000012088.1};
OS   Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS   coquereli).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC   Indriidae; Propithecus.
OX   NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000012088.1, ECO:0000313|Proteomes:UP000233160};
RN   [1] {ECO:0000313|Ensembl:ENSPCOP00000012088.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore
CC       {ECO:0000256|ARBA:ARBA00004629}.
CC   -!- SIMILARITY: Belongs to the TOG/XMAP215 family.
CC       {ECO:0000256|ARBA:ARBA00025722}.
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DR   RefSeq; XP_012500554.1; XM_012645100.1.
DR   STRING; 379532.ENSPCOP00000012088; -.
DR   Ensembl; ENSPCOT00000022680.1; ENSPCOP00000012088.1; ENSPCOG00000017517.1.
DR   GeneID; 105811021; -.
DR   KEGG; pcoq:105811021; -.
DR   CTD; 9793; -.
DR   GeneTree; ENSGT00390000014757; -.
DR   OrthoDB; 5477703at2759; -.
DR   Proteomes; UP000233160; Unplaced.
DR   GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR   GO; GO:0035371; C:microtubule plus-end; IEA:Ensembl.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR   GO; GO:0000922; C:spindle pole; IEA:Ensembl.
DR   GO; GO:0061863; F:microtubule plus end polymerase; IEA:InterPro.
DR   GO; GO:0051010; F:microtubule plus-end binding; IEA:InterPro.
DR   GO; GO:0043021; F:ribonucleoprotein complex binding; IEA:Ensembl.
DR   GO; GO:0007098; P:centrosome cycle; IEA:Ensembl.
DR   GO; GO:0030951; P:establishment or maintenance of microtubule cytoskeleton polarity; IEA:Ensembl.
DR   GO; GO:0046785; P:microtubule polymerization; IEA:InterPro.
DR   GO; GO:0090063; P:positive regulation of microtubule nucleation; IEA:Ensembl.
DR   GO; GO:0007051; P:spindle organization; IEA:Ensembl.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 5.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR024395; CLASP_N_dom.
DR   InterPro; IPR021133; HEAT_type_2.
DR   InterPro; IPR034085; TOG.
DR   InterPro; IPR045110; XMAP215.
DR   InterPro; IPR048491; XMAP215_CLASP_TOG.
DR   PANTHER; PTHR12609:SF0; CYTOSKELETON-ASSOCIATED PROTEIN 5; 1.
DR   PANTHER; PTHR12609; MICROTUBULE ASSOCIATED PROTEIN XMAP215; 1.
DR   Pfam; PF12348; CLASP_N; 1.
DR   Pfam; PF21041; XMAP215_CLASP_TOG; 4.
DR   SMART; SM01349; TOG; 5.
DR   SUPFAM; SSF48371; ARM repeat; 2.
DR   PROSITE; PS50077; HEAT_REPEAT; 1.
PE   3: Inferred from homology;
KW   Centromere {ECO:0000256|ARBA:ARBA00023328};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Kinetochore {ECO:0000256|ARBA:ARBA00022838};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233160};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          1..227
FT                   /note="TOG"
FT                   /evidence="ECO:0000259|SMART:SM01349"
FT   DOMAIN          269..472
FT                   /note="TOG"
FT                   /evidence="ECO:0000259|SMART:SM01349"
FT   REPEAT          405..443
FT                   /note="HEAT"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT   DOMAIN          551..783
FT                   /note="TOG"
FT                   /evidence="ECO:0000259|SMART:SM01349"
FT   DOMAIN          815..1047
FT                   /note="TOG"
FT                   /evidence="ECO:0000259|SMART:SM01349"
FT   DOMAIN          1156..1394
FT                   /note="TOG"
FT                   /evidence="ECO:0000259|SMART:SM01349"
FT   REGION          481..544
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          776..815
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1042..1120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1386..1409
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1766..1787
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1914..1998
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1931..1946
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1947..1962
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1963..1983
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1998 AA;  221928 MW;  3DB29EF3120CFD35 CRC64;
     MGDDSEWLKL PVDQKCEHKL WKARLSGYEE ALKIFQKIKD EKSPEWSKFL GLIKKFVTDS
     NAVVQLKGLE AALVYVENAH VAGKTTGEVV SGVVSKVFNQ PKAKAKELGI EICLMYIEIE
     KGEAVQEELL KGLDNKNPKI VVACIETLRK ALSEFGSKII LLKPIIKVLP KLFESREKAI
     RDEAKLIAVE IYRWIRDALR PPLQNINSVQ LKELEEEWVR LPTGAPKPSR FLRSQQELEA
     KLELQQSAGG DAEGGGDDGD EVPQIDAYEL LEAVEVLSKL PKDFYDKIEA KKWQERKEAL
     EAVEVLVKNP KLEAGDYADL VKALKKVVPT ILEKFKEKKP QVVQALQEAI DAIFLTTTLQ
     NISEDVLAVM DNKNPTIKQQ TSLFIARSFR HCTASTLPKS LLKPFCAALL KHINDSAPEV
     RDAAFEALGT ALKVVGEKAV NPFLADVDKL KLDKIKECSE KVELVHGKKA GLAADKKEFK
     PVPGRTAASG AAGDKDMKDI SAPKPGPLKK APATKAGGPP KKGKPTAPGG TGSTGTKNKK
     GLETKEIVEP ELSIEVCEEK ASVVLPPTCI QVLDSSNWKE RLACMEEFQK AVELMDRTEM
     PCQALVRMLA KKPGWKETNF QVMQMKLHIV ALIAQKGNFS KTSAQIVLDG LVDKIGDVKC
     GNNAKEAMTA IAEACMLPWT AEQVMSMAFS QKNPKNQSET LNWLSNAIKE FGFSGLNVKA
     FISNVKTALA ATNPAVRTSA ITLLGVMYLY VGPSLRMFFE DEKPALLSQI DAEFEKMQGQ
     SPPAPTRGIS KHSTSGTDEG EDGDEPDDGG NDVVDLLPRT EISDKITSEL VSKIGDKNWK
     IRKEGLDEVA GIINEAKFIQ PNIGELPTAL KGRLNDSNKI LVQQTLNILQ QLAVAMGPNI
     KQHVKNLGIP IITVLGDSKN NVRAAALATV NAWAEQTGMK EWLEGEDLSE ELKKENPFLR
     QELLGWLAEK LPSLRSTPTD LILCVPHLYS CLEDRNGDVR KKAQDALPFF MMHLGYEKMA
     KATGKLKPTS KDQVLAMLEK AKANMPAKPA APTKATSKPM GGSAPAKFQP ASAPAEDSVS
     SSAEPRPDPK KAKAPGVSSK AKSAQGKKVP SKTSLKEDED KSGPIFIVVP NGKEQRMKDE
     KGLKVLKWNF TTPRDEYIEQ LKTQMSSCVA KWLQDEMFHS DFQHHNKALA VMVDHLESEK
     EGVIGCLDLI LKWLTLRFFD TNTSVLMKAL EYLKLLFTLL SEEEYHLTEN EASSFIPYLI
     LKVGEPKDVI RKDVRAILNR MCLVYPASKM FPFIMEGTKS KNSKQRAECL EELGCLVESY
     GMNVCQPTPG KALKEIAIHI GDRDNAVRNA ALNTIVTVYN VHGDQVFKLI GNLSEKDMSM
     LEERIKRSAK RPSAAPIKQV EEKPQRTQSI SSNANMLRKG PAEDMSSKLN QARSMSGHPE
     AAQMVRREFQ LDLDEIENDN GTVRCEMPEL VQHKLDDIFE PVLIPEPKIR AVSPHFDDMH
     SNTASTINFI ISQVASGDIN TSIQALTQID EVLRQEDKAE AMSGHIDQFL IATFMQLRLI
     YNTHMADEKL EKDEIIKLYS CIIGNMISLF QIESLAREAS TGVLKDLMHG LITLMLDSRI
     EDLEEGQQVI RSVNLLVVKV LEKSDQTNIL SALLVLLQDS LLATASSPKF SELVMKCLWR
     MVRLLPDTIN SINLDRILLD IHIFMKVFPK EKLKQCKSEF PIRTLKTLLH TLCKLKGPKI
     LDHLTMIDNK NESELEAHLC RMMKHSMDQT GSKSDKETEK GASRLDEKSS KAKVNDFLAE
     IFKKIGSKEN TKEGLAELYE YKKKYSDADI EPFLKNSSQF FQSYVERGLR VIEMEREGKG
     RIPTSTGISP QMEVTCVPTP TSTVSSIGNT NGEEVGPSVY LERLKILRQR CGLDNAKQDD
     RPPLTSLLSK PAVPTVASST DMLHSKLSQL RESREQHQHS DLDSNQIHSS GTMTTSSSST
     ANIDDLKKRL ERIKSSRK
//
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