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Database: UniProt
Entry: A0A452SNV8_URSAM
LinkDB: A0A452SNV8_URSAM
Original site: A0A452SNV8_URSAM 
ID   A0A452SNV8_URSAM        Unreviewed;      1633 AA.
AC   A0A452SNV8;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Cytoskeleton associated protein 5 {ECO:0000313|Ensembl:ENSUAMP00000034372.1};
GN   Name=CKAP5 {ECO:0000313|Ensembl:ENSUAMP00000034372.1};
OS   Ursus americanus (American black bear) (Euarctos americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX   NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000034372.1, ECO:0000313|Proteomes:UP000291022};
RN   [1] {ECO:0000313|Proteomes:UP000291022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA   Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT   "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT   in black bear kidneys.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSUAMP00000034372.1}
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   Ensembl; ENSUAMT00000038278.1; ENSUAMP00000034372.1; ENSUAMG00000025271.1.
DR   GeneTree; ENSGT00390000014757; -.
DR   Proteomes; UP000291022; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
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:0030951; P:establishment or maintenance of microtubule cytoskeleton polarity; IEA:InterPro.
DR   GO; GO:0046785; P:microtubule polymerization; IEA:InterPro.
DR   GO; GO:0051128; P:regulation of cellular component organization; IEA:UniProt.
DR   GO; GO:0007051; P:spindle organization; IEA:InterPro.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 4.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR024395; CLASP_N_dom.
DR   InterPro; IPR000357; HEAT.
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; PF02985; HEAT; 1.
DR   Pfam; PF21041; XMAP215_CLASP_TOG; 2.
DR   SMART; SM01349; TOG; 4.
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   Kinetochore {ECO:0000256|ARBA:ARBA00022838};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291022};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          1..192
FT                   /note="TOG"
FT                   /evidence="ECO:0000259|SMART:SM01349"
FT   REPEAT          129..167
FT                   /note="HEAT"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT   DOMAIN          214..446
FT                   /note="TOG"
FT                   /evidence="ECO:0000259|SMART:SM01349"
FT   DOMAIN          478..710
FT                   /note="TOG"
FT                   /evidence="ECO:0000259|SMART:SM01349"
FT   DOMAIN          821..1059
FT                   /note="TOG"
FT                   /evidence="ECO:0000259|SMART:SM01349"
FT   REGION          179..205
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          439..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          708..735
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1050..1091
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1420..1441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1549..1633
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1069..1085
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1582..1597
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1598..1618
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1633 AA;  181747 MW;  3CE89E2B2E044946 CRC64;
     MLCIRDCLIE GIWKEVVGKD TNVMLVALAA KCLTGLAVGL RKKFGQYAGH VVPTILEKFK
     EKKPQVVQAL QEAIDAIFLT TTLQNISEDV LAVMDNKNPT IKQQTSLFIA RSFRHCTAST
     LPKSLLKPFC AALLKHINDS APEVRDAAFE ALGTALKVVG EKAVNPFLAD VDKLKLDKAG
     GPPKKGKTAA PGGAGSAGTK NKKGLETKEI VEPELSIEVC EEKASAVLPA TCIQLLDSSN
     WKERLACMEE FQKAVELMDR TEMPCQALVR MLAKKPGWKE TNFQVMQMKL HIVALIAQKG
     NFSKTSAQIV LDGLVDKIGD VKCGNNAKEA MTAIAEACML PWTAEQVMSM AFSQKNPKNQ
     SETLNWLSNA IKEFGFSGLN VKAFISNVKT ALAATNPAVR TSAITLLGVM YLYVGPSLRM
     FFEDEKPALL SQIDAEFEKM QGQSPPAPTR GISKHSISGT DEGEDGDEPD EVGTDVVDLL
     PRTEISDKIT SELVSKIGDK NWKIRKEGLD EVAAIINEAK FIQPNIGELP TALKGRLNDS
     NKILVQQTLN ILQQLAVAMG PNIKQHVKNL GIPIITVLGD SKNNVRAAAL ATVNAWAEQT
     GMKEWLEGED LSEELKKENP FLRQELLGWL AEKLPTLRST PTDLILCVPH LYSCLEDRNG
     DVRKKAQDAL PFFMMHLGYE KMAKATGKLK PTSKDQVLAM LEKAKANMPA KPAASAKATS
     KPVGGSAPAK FQPASGNSIL RGLREKEVAQ GNSKKKSSLH FLPYFQTSAQ GKKVPSKTSL
     KEDEDKSGPI FIVVPNGKEQ RMKDEKGLKV LKWNFTTPRD EYIEQLKTQM SSCVAKWLQD
     EMFHSDFQHH NKALAVMVDH LESEKEGVIG CLDLILKWLT LRFFDTNTSV LMKALEYLKL
     LFTLLSEEEY HLTENEASSF IPYLILKVGE PKDVIRKDVR AILNRMCLVY PASKMFPFIM
     EGTKSKNSKQ RAECLEELGC LVESYGMNVC QPTPGKALKE IAIHIGDRDN AVRNAALNTI
     VTVYNVHGDQ VFKLIGTLSE KDMSMLEERI KRSAKRPSAA PVKQVEEKPP RTQSVNSNAS
     MQRKGPAEDM SSKLNQARSM SGHPEAAQMV RREFQLDLDE IENDNGTVRC EMPELVQHKL
     DDIFEPVLIP EPKIRAVSPH FDDMHSNTAS TINFIISQVA SGDINTSIQA LTQIDEVLRQ
     EDKAEAMSGH IDQFLIATFM QLRLIYNTHM ADEKLEKDEI IKLYSCIIGN MISLFQIESL
     AREASTGVLK DLMHGLITLM LDSRIEDLEE GQQVIRSVNL LVVKVLEKSD QTNILSLGQV
     NGDRNSLHSS CLWRMVRLLP DTINSINLDR ILLDIHIFMK VFPKEKLKQC KSEFPIRTLK
     TLLHTLCKLK GPKILDHLTM IDNKNESELE AHLCRMMKHS MDQTGSKSEK ETEKGASRID
     EKSSKAKVND FLAEIFKKIG SKENTKEGLA ELYEYKKKYS DADIEPFLKN SSQFFQSYVE
     RGLRVIEMER EGKGRIPTST GMASSSEEVG PSVYLERLKI LRQRCGLDNT KVQDERPPLT
     SLLSKPAVPP VASSTDMLHS KLSQLRESRE QHQHSDLDSN QTHSSGTMTT SSSSTANIDD
     LKKRLERIKS SRK
//
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