ID A0A452SSS0_URSAM Unreviewed; 1325 AA.
AC A0A452SSS0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Cytoplasmic linker associated protein 2 {ECO:0000313|Ensembl:ENSUAMP00000035942.1};
GN Name=CLASP2 {ECO:0000313|Ensembl:ENSUAMP00000035942.1};
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:ENSUAMP00000035942.1, 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:ENSUAMP00000035942.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore
CC {ECO:0000256|ARBA:ARBA00004629}. Golgi apparatus, trans-Golgi network
CC {ECO:0000256|ARBA:ARBA00004601}.
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DR Ensembl; ENSUAMT00000040011.1; ENSUAMP00000035942.1; ENSUAMG00000022209.1.
DR GeneTree; ENSGT00940000155574; -.
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:0015630; C:microtubule cytoskeleton; IEA:UniProt.
DR GO; GO:0008017; F:microtubule binding; IEA:UniProt.
DR GO; GO:0051494; P:negative regulation of cytoskeleton organization; IEA:UniProt.
DR GO; GO:1902904; P:negative regulation of supramolecular fiber organization; IEA:UniProt.
DR GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; IEA:UniProt.
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; IPR021133; HEAT_type_2.
DR InterPro; IPR034085; TOG.
DR InterPro; IPR048491; XMAP215_CLASP_TOG.
DR PANTHER; PTHR21567; CLASP; 1.
DR PANTHER; PTHR21567:SF30; CLIP-ASSOCIATING PROTEIN 2; 1.
DR Pfam; PF21040; CEP104-like_TOG; 1.
DR Pfam; PF12348; CLASP_N; 1.
DR Pfam; PF21041; XMAP215_CLASP_TOG; 1.
DR SMART; SM01349; TOG; 4.
DR SUPFAM; SSF48371; ARM repeat; 2.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
PE 4: Predicted;
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:UP000291022};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1325
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019139786"
FT DOMAIN 2..151
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT REPEAT 91..129
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT DOMAIN 205..438
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT DOMAIN 687..924
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT DOMAIN 1078..1318
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT REGION 160..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 917..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 991..1028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..685
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1016
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1325 AA; 146236 MW; 91A53FFD33281BB5 CRC64;
MEMNYEYLLS FSCLSLVIVA LIDRMGDAKD KVRDEAQTLI LKLMDQVAPY IWEQLASGFK
HKNFRSREGV CLCLIETLNI FGAQPLVLSK LVPHLCILFG DSNSQVRDAA VLAIVEIYRH
VGERVRVDLC KRGIPPQSLV LLIYIFLMLC ADKSFDDEES VDGNRPSSTA SAFKVPAPKT
SGNPVNSARK PGSAGGPKVG GNIYSSRELE ETLNKIREIL SDDKHDWDQR ANALKKIRSL
LVAGAAQYDC FFQHLRLLDG ALKLSAKDLR SQVVREACIT VAHLSTVLGN KFDHGAEAIV
PTLFNLVPNS AKVMATSGCA AIRFIIRHTH VPRLIPLITS NCTSKSVPVR RRSFEFLDLL
LQEWQTHSLE RHAAVLVETI KKGIHDADAE ARVEARKTYM GLRNHFPGEA ETLYNSLEPS
YQKSLQTYLK SSGSVASLPQ SDRSSSSSQE SLNSKASSLP GSLQRSRSDI DVNAAAGAKA
HHAAGQSVRS GRLGAGALNP GSYASLGKTS SHLNISMYVW CSAGSRSGSP GRVLTTTALS
TVSSGVQRVL VNSASAPKRS KIPRSQGCSR EASPSRLSVA RSSRIPRPSV SQGCSREASR
ESSRDTSPVR SFQPLGNQSS RLSSSVSAMR VLNTGSDVEE AVADALKKPA RRRYESYGMH
SDDDANSDAS SACSERSYSS RNGSIPTYMR QTEDVAEVLN RCASSNWSER KEGLLGLQNL
LKNQRTLSRV ELKRLCEIFT RMFADPHGKV FSMFLETLVD FIQVHKDDLQ DWLFVLLTQL
LKKMGADLLG SVQAKVQKAL DVTRESFPND LQFNILMRFT VDQTQTPSLK VKVAILKYIE
TLAKQMDPGD FINSSETRLA VSRVITWTTE PKSSDVRKAA QSVLISLFEL NTPEFTMLLG
ALPKTFQDGA TKLLHNHLRN TGNGTQGPMG SPLTRPTPRS PANWSSPLTS PTNTSQNTLS
PSAFDYDTEN MNSEDIYSSL RGVTEAIQNF SFRSQEDMNE PLKRDSKKDD SDSVRGDATD
SSQTALDNKA SLLHSMPAHS SPRARDYNPY NYSDSLSPFN KSALKEAMFD DDADQFPDGR
FWVILYHSDL VAELLKELSN HNERVEERKI ALYELMKLTQ EESFGVWDEH FKTILLLLLE
TLGDKEPTIR ALALKVLREI LRHQPARFKN YAELTVMKTL EAHKDPHKEV VRSAEEAASV
LATSISPEQC IKVLCPIIQT ADYPINLAAI KMQTKVIERV SKETLNLLLP EIMPGLIQGY
DNSESSVRKA CVFCLVAVHA VIGDELKPHL SQLTGSKMKL LNLYIKRAQT GSGGADPTTD
VSGQS
//
