ID F1KQ68_ASCSU Unreviewed; 1923 AA.
AC F1KQ68;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Ankyrin-1 {ECO:0000313|EMBL:ADY40022.1};
OS Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX NCBI_TaxID=6253 {ECO:0000313|EMBL:ADY40022.1};
RN [1] {ECO:0000313|EMBL:ADY40022.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21685128; DOI=10.1101/gr.121426.111;
RA Wang J., Czech B., Crunk A., Wallace A., Mitreva M., Hannon G.J.,
RA Davis R.E.;
RT "Deep small RNA sequencing from the nematode Ascaris reveals conservation,
RT functional diversification, and novel developmental profiles.";
RL Genome Res. 21:1462-1477(2011).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}.
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DR EMBL; JI164089; ADY40022.1; -; mRNA.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051179; P:localization; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd08317; Death_ank; 1.
DR Gene3D; 2.60.220.30; -; 2.
DR Gene3D; 2.60.40.2660; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
DR Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR040745; Ankyrin_UPA.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR000488; Death_domain.
DR InterPro; IPR000906; ZU5_dom.
DR PANTHER; PTHR24123:SF33; ANKYRIN 2, ISOFORM U; 1.
DR PANTHER; PTHR24123; ANKYRIN REPEAT-CONTAINING; 1.
DR Pfam; PF00023; Ank; 4.
DR Pfam; PF12796; Ank_2; 7.
DR Pfam; PF00531; Death; 1.
DR Pfam; PF17809; UPA_2; 1.
DR Pfam; PF00791; ZU5; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 23.
DR SMART; SM00005; DEATH; 1.
DR SMART; SM00218; ZU5; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 3.
DR SUPFAM; SSF47986; DEATH domain; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 20.
DR PROSITE; PS50088; ANK_REPEAT; 21.
DR PROSITE; PS50017; DEATH_DOMAIN; 1.
DR PROSITE; PS51145; ZU5; 2.
PE 2: Evidence at transcript level;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REPEAT 61..93
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 94..126
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 127..159
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 160..183
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 222..254
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 255..287
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 288..320
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 321..353
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 354..386
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 387..419
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 420..452
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 453..485
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 486..518
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 519..551
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 552..584
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 585..617
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 618..650
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 651..683
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 684..716
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 717..749
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 750..782
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 994..1151
FT /note="ZU5"
FT /evidence="ECO:0000259|PROSITE:PS51145"
FT DOMAIN 1153..1297
FT /note="ZU5"
FT /evidence="ECO:0000259|PROSITE:PS51145"
FT DOMAIN 1502..1572
FT /note="Death"
FT /evidence="ECO:0000259|PROSITE:PS50017"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1575..1599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1618..1639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1736..1859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1899..1923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1582..1599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1619..1639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1736..1764
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1776..1819
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1923 AA; 209985 MW; 7E85E7724C0509D5 CRC64;
MTDLGGEGAG SPNPQPAADN GQHSNKGESS ASFLRAARAG NLERVLELLR SGTDINTCNA
NGLNALHLAS KEGHHEVVRE LLKRKALVDA ATKKGNTALH IASLAGQEVI VTILVENGAN
VNVQSLNGFT PLYMAAQENH ESVVRYLLAH GANQALATED GFTPLAVALQ QGHDRVVALL
LENDTRGKVR LPALHIAAKK DDTKAATLLL QNEHNADVTS KSGFTPLHIA AHYGNENVAQ
LLLEKGANVN YQARHNISPL HVATKWGRAN MVSLLLAHGA VIDCRTRDLL TPLHCAARSG
HDQVVDLLLE KGAPINAKTK NGLAPLHMAA QGDHVDTARI LLYHRAPVDD VTVDYLTPLH
VAAHCGHVRV AKLLLDRNAD PNARALNGFT PLHIACKKNR IKVVELLLKY HAAIEATTES
GLSPLHVAAF MGAINIVIYL LQQGANADVA TVRGETPLHL AARANQTDIV RVLVRDGAKV
DAAARELQTP LHIASRLGNT DIVVLLLQAG ASPNAATRDQ YTPLHIAAKE GQEEVAAILL
DRGADKTLLT KKGFTPLHLA AKYGNLQVAK LLLERGTPVD IEGKNQVTPL HVAAHYNNDK
VALLLLENGA SAHAAAKNGY TPLHIAAKKN QMDIATTLLH YKADTNAESK AGFSPLHLAA
QEGHREMCAL LIENGAKVGA TAKNGLTPMH LCAQEDRVNV AEELVKEHAA IDPQTKAGYT
PLHVACHFGQ MNMVRFLIEH GAPVSATTRA SYTPLHQAAQ QGHNNVVRYL LEHGASPNVH
TATGQTPLSI AERLGYVSVV EALKTVTETT VITETTTITE ERYKPQNPEA MNETMFSDSE
DEATAAALDE DPSHLRALTH SPLRLSTSDD HDLSFFPNHT SSPYPSPAGE FKLAPSREDN
QVTANAHVRD FSESLTQGLH DSTGVHLIHT AEPLLSRSPE MDTADGDLDA LIRKAQHEPV
ATAMADSTLD ATIPDNVALT HTTVQPSKLL HKTFLISFMV DARGGAMRGC RHSGVRIIIP
PRKASQPMRI TCRYLRRDKL AHPPPLSEGE ALASRVLEMA PHGAKFLGPV ILEVPHFASL
RGREREIVIL RSDDGQHWKE HQLEATEDAV QEVLNESFDA EELSQLDDLH TTRITRILTN
DFPMYFAVVT RVRQEVHCVG PEGGVILSSV VPRVQAIFPD GSLTKTIKVS VQAQPVPHEI
VTRLHGNRVA VSPIVTVEPR RRKFHKPITL CIPLPQSAHK GMLTQYSGQP GQEPPTLRLL
CSITGGSAPA QWEDITGTTQ LTFTGEDVSF TTTVSARFWL MDCQTPRDAA RMAQEVYNEA
IAVPYMAKFV IFARRTFPTE GQLRVFCMTD DREDKTLEKQ EHFIEIAKSK DVEVLSGRHQ
FLEFAGNIMP VTKSGDQLSL YFLPFQENRL AFLIRVRSQE DEEAAAGGRI AFMKEPKARA
DSLPPQQPLC TLAITLPDYT GQGTPLSALS TEAPSIAAKY SQSLRETSDP PGLPISHVSR
LIGADWHRLA RALEVPDTDI RHVRQQMVGR ESITILRIWI YLKKEYATPD ALRTALRRIG
REDVLREMGK DEKAIDMDAS SASHASLPTT TASTSTGPVT AATASVTRAY VQAEEPFTED
VSVSHSTAAP SYQTTPEVQL ARASTADAYV AEPLSQAIVQ EEDEEVPVSE IRTVVRTERH
VHDSENGPIV EERTITTTYE DDVAINEEVV DRIVPLNAEE QEKWDRMVRE AQDALERQEP
LQSDDGTHRE VYQEEHERED GTIVKTTTVK TSHITREEPQ WSDHYEKQEP PKTHTDVSSH
VSEAVEKGRD AEDAKGRVLE NEGSATAPPS AHPDTAKPVT DQKHESMAEG FTSEDGSTVV
SKKMTRVVTT TRTTLPGDTN EQNAGDLIRL KVNEQVYSGS VDPSDQHIHL VPITKVDQPS
QPQ
//
