ID E4XMP2_OIKDI Unreviewed; 2671 AA.
AC E4XMP2;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=KASH domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=GSOID_T00015436001 {ECO:0000313|EMBL:CBY19784.1};
OS Oikopleura dioica (Tunicate).
OC Eukaryota; Metazoa; Chordata; Tunicata; Appendicularia; Copelata;
OC Oikopleuridae; Oikopleura.
OX NCBI_TaxID=34765 {ECO:0000313|EMBL:CBY19784.1};
RN [1] {ECO:0000313|EMBL:CBY19784.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21097902; DOI=10.1126/science.1194167;
RA Denoeud F., Henriet S., Mungpakdee S., Aury J.M., Da Silva C.,
RA Brinkmann H., Mikhaleva J., Olsen L.C., Jubin C., Canestro C.,
RA Bouquet J.M., Danks G., Poulain J., Campsteijn C., Adamski M., Cross I.,
RA Yadetie F., Muffato M., Louis A., Butcher S., Tsagkogeorga G., Konrad A.,
RA Singh S., Jensen M.F., Cong E.H., Eikeseth-Otteraa H., Noel B.,
RA Anthouard V., Porcel B.M., Kachouri-Lafond R., Nishino A., Ugolini M.,
RA Chourrout P., Nishida H., Aasland R., Huzurbazar S., Westhof E., Delsuc F.,
RA Lehrach H., Reinhardt R., Weissenbach J., Roy S.W., Artiguenave F.,
RA Postlethwait J.H., Manak J.R., Thompson E.M., Jaillon O., Du Pasquier L.,
RA Boudinot P., Liberles D.A., Volff J.N., Philippe H., Lenhard B.,
RA Roest Crollius H., Wincker P., Chourrout D.;
RT "Plasticity of animal genome architecture unmasked by rapid evolution of a
RT pelagic tunicate.";
RL Science 330:1381-1385(2010).
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DR EMBL; FN653079; CBY19784.1; -; Genomic_DNA.
DR InParanoid; E4XMP2; -.
DR Proteomes; UP000001307; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; IEA:InterPro.
DR CDD; cd00051; EFh; 1.
DR CDD; cd00176; SPEC; 4.
DR Gene3D; 1.20.58.60; -; 11.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 3.30.920.20; Gas2-like domain; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR003108; GAR_dom.
DR InterPro; IPR036534; GAR_dom_sf.
DR InterPro; IPR043197; Plakin.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR PANTHER; PTHR23169; ENVOPLAKIN; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF02187; GAS2; 1.
DR Pfam; PF00435; Spectrin; 1.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00243; GAS2; 1.
DR SMART; SM00150; SPEC; 7.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF143575; GAS2 domain-like; 1.
DR SUPFAM; SSF46966; Spectrin repeat; 9.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS51460; GAR; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Reference proteome {ECO:0000313|Proteomes:UP000001307}.
FT DOMAIN 2321..2356
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 2360..2432
FT /note="GAR"
FT /evidence="ECO:0000259|PROSITE:PS51460"
FT REGION 304..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2487..2654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 117..255
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 496..530
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 775..828
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1101..1145
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1231..1361
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1412..1446
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1548..1582
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 306..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2487..2504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2557..2594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2602..2647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2671 AA; 303876 MW; E08540979FCF9F06 CRC64;
MKELNLIANR GCKMPKFAFL LWAPQAGSQD PSFEIPIKKE ITTNSSTDLA TLNEQIIDAK
TARHDADGHK NAFKRLDQTA RAIGRLGDEL VSHRDQQRVL RQTQKLRQGF QALSDKIDMK
VKELVEMGNE LQQLQEKITN ANNEAEVATR VLKEVSRAAR ADKNLLEERK DRLKLSQTEI
KRAEREIKES GEKAALKVLS KCGEENARAV REKLANAQRR IEEVAENIEK EERKLSRMIE
LLSDFESHAD HLENEIQTLQ NPKACEVKLG NLREAASHLL DCGNFSDHSP VTLRLDRLNR
MLTNASEQSR ERRNALENEK RRETEREREF ENVKMDLGQF DVVSIQSLAN LPADLNKLDN
LITKWENLEP KLEYLESTSE SPIMQPGSTA SLRRRSRTRR QGGTLPRNSG RLSGPSASGV
EGLRLKYESI GDRLINTRNV GQILLEQLEV WHSNQVKAEH IMKNLADSSS LISAMGDVAE
AVRSGKAVIT TCRTKLDNEP KDLPKLETEV DQLQNQFNEA QQKIMDARLS KDQKSKDIDH
WQQRFLNLSD WTSDQWSLMS VLGKISADPA ILEPQRQQVD ALLSEFNSRK DRYNQLQADC
LSLNDTSKSQ DMKQLSSRWN ELEQKLEERK IAIDEALKCT REIEQETAKL QDFLTTVTAD
LAISSRLPPA PDSVEDCLKK LRRHQTCVPE MEKSAKLAQQ AAEFLAQVAA GAENHGNKSH
SVGQALFIST KKLDEKIGTL TELLVNIDEA YKLRSGLFNS INCIEKAATY GREEVNALRS
KYDELVALVE EISENTSPIR NNSLREDKRA IQRKIKALET GLDQRERDES RRARKQAQLL
SFINDREQQI ASTHQGETQP DSIHQKITLV QTLKDELNAR MGELKAQFGG PTDSQVQQSF
NCLLEKSNDR AKELQDAKLQ AEELDGLLHD FNEWAEDSLE KILAATNFKS PETLYEMQAM
MEECKEQRGE IELICSLLKG VEPAGKRWSG RPLEQVHTDA LHTLDRIRSL LSERTEAADD
ALNRVKRFED SVEKLTAWYR EIGEDLEKTK SAVDLTEPAI IDKMVDDVGR ISTILQSKMA
TREIMSRECQ TMNFDLADGM KDSVQEKLAK LETTASGTEL KCRELQNLLE KIQRASTKYA
EVRDELLPWI EDMEVRLDQF DEVSLPDEIL IEELSQMSEK IAERRLLADR LVTTADKLAP
LGALQVKNEA AQISSRYSDI RERCRQRKRE TQQLAIEHQQ YSDRLNNLNN ALHRIDERLS
NSDRPECNVE KCRAAMADLN QLSKELAKLE AAKTTLQKAG ENQLSDPKIR SELNKIDATW
DHLQNTLKSK QERLRQAEAA SERFAAKNSQ FQNELDQLEG ELRNIKPTHD GKRDMDQFEK
KITAMTGLNK KVSDAARDLG SLGQNAEALR MAREGQTQLD RIARNMQQKQ NEIEAAAKDH
ENMQRKAREA LSWMQSADVR LKAQGEPNSP DDCREKLRVI SDIKNQAPKF AAALPASSWR
QFENRLADEV RDTENKLLSM GHFDQALDEI SDWTSRCSTT LSSIGQDANA LQTDFARAEL
IMSELESRHR ALEKLRETAV ERFPLKQKRL VAIADNLSKI GSIASTKHDV IRSRIEAAES
TELRKKKVQR WAADIREYLI NDGPYSGSSE GARAQSDECR NKISEMAKQR GECPAALPDV
RWQQMETALS ERKNKLGNLQ LEVDTFWDAA KKLDKSLGQF ESQIQKMQPP SVVEDSTNLQ
IEQNRKLEDD IRLKTNLVKT IEDLSGSLRV NINREDAIQV KNAALTIHSR WEKCLQATNR
RNLALEENRK RATKYSEMVI ELIDFMDLSR SKLEEAKSSC DPRNGKRLLT KHSEIEREIA
RNEKGYDKVK KEAAHLLKIA KLPSDISAIE VELKEIQHKW GSLQNLSWNF VKDLQDSMVS
SGRLIDALES LEEWLIRVEP ELSERRPLEG DLDTVERLLE NHRDFKRELE ERERSFSDIR
RLVVDLSEQD AAWMRPQISG LGSRWENLRT LSRRRDDKLA RAKVRAQEFQ DEVNNTLNWL
AIAEERLDNI AMLLDGDTSG SLLDKAKRNQ GDLVQDMEKN KSQLERAVQL GNGILTNADP
DAVGTLKHWM GALSAGWQEV QAWIEQLGER IARMENDEAD AQERLDTLLN WLTGAQDQLA
IRNRTPLPSE TLRLKQLAAE HQQFQEEILA RQTEFDELIR IYKKNTNSNV MRESYGSLKR
NTKITHQGLV EFKNSKAALL SGTWQSVWLA ALERQRAIAN ALDGAEENQF DFDTWRKRYM
AWMNHKKSRV METMRSFDKK NTGFIENRRF INGVIDSGFD TNEREMRKVV NMFDRDGNGQ
VDYYEFISAL HPRDQYKPDS DAAKIEDEVI REVSRCRCCE RFAIHQISDN KYRFGDSQQL
RLVRILKSTV MVRVGGGWMA LEEFLSKNDP CRGASRKKWA SSKRLIRCNS DLSLPSSFSV
DTSSSGETFS QSGLLVGHFG GSLTDLDQSE SLSQTGSSMS ACSDLPRIKG SKLPLRTRGK
VAPKSDGYPT DPLADGVSQT MSAFSRKSRR DRHNSTSSQQ PIRTTATDRP NTRPGSRIPS
RNPSRSNSRA GSRAGSRDPS PHNRIPNLSV LSPKSLTPQG LVSPMSHRSS GRKTPSGYKT
PSGRRTPNGD SDIAEAARRL YTLQTERNSK S
//
