ID F1KQE2_ASCSU Unreviewed; 1839 AA.
AC F1KQE2;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Ankyrin-2 {ECO:0000313|EMBL:ADY40096.1};
DE Flags: Fragment;
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:ADY40096.1};
RN [1] {ECO:0000313|EMBL:ADY40096.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JI164185; ADY40096.1; -; mRNA.
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:0009605; P:response to external stimulus; 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|PROSITE-ProRule:PRU00023};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
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 1010..1167
FT /note="ZU5"
FT /evidence="ECO:0000259|PROSITE:PS51145"
FT DOMAIN 1169..1313
FT /note="ZU5"
FT /evidence="ECO:0000259|PROSITE:PS51145"
FT DOMAIN 1518..1588
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 1591..1615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1634..1655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1785..1839
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 1598..1615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1635..1655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1792..1839
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1839
FT /evidence="ECO:0000313|EMBL:ADY40096.1"
SQ SEQUENCE 1839 AA; 201011 MW; 44BB2F997E9EE5C4 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 HTTVQPRTIP DNVALTHTTV QPSKLLHKTF LISFMVDARG
GAMRGCRHSG VRIIIPPRKA SQPMRITCRY LRRDKLAHPP PLSEGEALAS RVLEMAPHGA
KFLGPVILEV PHFASLRGRE REIVILRSDD GQHWKEHQLE ATEDAVQEVL NESFDAEELS
QLDDLHTTRI TRILTNDFPM YFAVVTRVRQ EVHCVGPEGG VILSSVVPRV QAIFPDGSLT
KTIKVSVQAQ PVPHEIVTRL HGNRVAVSPI VTVEPRRRKF HKPITLCIPL PQSAHKGMLT
QYSGQPGQEP PTLRLLCSIT GGSAPAQWED ITGTTQLTFT GEDVSFTTTV SARFWLMDCQ
TPRDAARMAQ EVYNEAIAVP YMAKFVIFAR RTFPTEGQLR VFCMTDDRED KTLEKQEHFI
EIAKSKDVEV LSGRHQFLEF AGNIMPVTKS GDQLSLYFLP FQENRLAFLI RVRSQEDEEA
AAGGRIAFMK EPKARADSLP PQQPLCTLAI TLPDYTGQGT PLSALSTEAP SIAAKYSQSL
RETSDPPGLP ISHVSRLIGA DWHRLARALE VPDTDIRHVR QQMVGRESIT ILRIWIYLKK
EYATPDALRT ALRRIGREDV LREMGKDEKA IDMDASSASH ASLPTTTAST STGPVTAATA
SVTRAYVQAE EPFTEDVSVS HSTAAPSYQT TPEVQLARAS TADAYVAEPL SQAIVQEEDE
EVPVSEIRTV VRTERHVHDS ENGPIVEERT ITTTYEDDVA INEEVVDRIV PLNAEEQEKW
DRMVREAQDA LERQEPLQSD DGTHREVYQE EHEREDGTIV KTTTVKTSHI TREEPQWSDH
YEKQEPPKTH TDVSSHVSEA VEKGRDAEDA KGRVLENEG
//