ID A0A1S3H3I8_LINUN Unreviewed; 860 AA.
AC A0A1S3H3I8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Ataxin-2-like protein isoform X7 {ECO:0000313|RefSeq:XP_013380041.1};
GN Name=LOC106151356 {ECO:0000313|RefSeq:XP_013380041.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013380041.1};
RN [1] {ECO:0000313|RefSeq:XP_013380041.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013380041.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the ataxin-2 family.
CC {ECO:0000256|ARBA:ARBA00007503}.
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DR RefSeq; XP_013380041.1; XM_013524587.1.
DR AlphaFoldDB; A0A1S3H3I8; -.
DR EnsemblMetazoa; XM_013524587.1; XP_013380041.1; LOC106151356.
DR GeneID; 106151356; -.
DR OrthoDB; 4269134at2759; -.
DR Proteomes; UP000085678; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR CDD; cd00600; Sm_like; 1.
DR InterPro; IPR009818; Ataxin-2_C.
DR InterPro; IPR045117; ATXN2-like.
DR InterPro; IPR009604; LsmAD_domain.
DR InterPro; IPR047575; Sm.
DR InterPro; IPR025852; SM_dom_ATX.
DR InterPro; IPR020891; UPF0758_CS.
DR PANTHER; PTHR12854; ATAXIN 2-RELATED; 1.
DR PANTHER; PTHR12854:SF7; ATAXIN-2 HOMOLOG; 1.
DR Pfam; PF06741; LsmAD; 1.
DR Pfam; PF07145; PAM2; 1.
DR Pfam; PF14438; SM-ATX; 1.
DR SMART; SM01272; LsmAD; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS52002; SM; 1.
DR PROSITE; PS01302; UPF0758; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000085678}.
FT DOMAIN 20..101
FT /note="Sm"
FT /evidence="ECO:0000259|PROSITE:PS52002"
FT REGION 215..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..452
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..663
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 860 AA; 93739 MW; EAD9D1CDFA1D4D7B CRC64;
MRGGQVDKAL YTEGVYGNAR FTHAVTSLVG CNVEVIVKNG GKYEGVMRTF SPKMEIVLEC
VHKIDDTVNN MVNTTPSKDQ IIDKVVFKTQ DILMLTALNV DMEYAYKDSF TDSAISKFNG
QVGEKELEPW EAEGPLCELG ALEGDSANGW DANDMFRTNA EVFNVKTSYD DSLTQYTTPL
ERKNTPEFRQ RQAEAARLAA EIESSDQYKA HIALEDTGSD EEDKFSAVVR PGESNHSGSK
SFRYVPPHRR SGPQTRGNRG GPSPTQVATQ QQQQQKPSTP TEETQPKMNG EKEEKKTEVD
TVSKTNNTEV SPQLPVEETS PGGTTSLPAP LPQSEKSAVK MDRRTNPTNQ KARQDQIKEL
KEFSTNFKLS DKDHSKEETG QQASPEKDKS SETSKAAPSD DKKSETATPE NKDDTVKKST
LNPNAKEFVF NPNAKPFQPK QAPTPPRPNS QSPLIQTPVF QQPMYQQFMP ANVAMSQMGM
AGMPQQPMLQ PGQQQRFVKR AEVSVNPRPN FSSQAAAANA VTGQPLMAQP GPNQATQFLP
AGVYPVQPMV HQGMVNPYPQ QVISMSNHNT GATPVMSTQQ LNMVPNSQGQ TEHGAQLLVQ
HPGASAVPAH MAAHHHGGHP HPQPAHMAPH HQGTPPHTAG GGGGQMTHQP GHPTPSPVQA
GGPQQMHPQH PPPSGTPQHV IFPAGPQAGQ QGQPVHPNTP TSPQPMHQVS FPYSYSTTMN
IPNNGSFMTI AHSQQSSTNT VHHQQHNHPS GQPQPQIVMM PQPQHQGQFG AATGQHPQLT
GNPQFQTPHM QGISRTVLIP SAYGTTPVSG PGPMHQVHPM VPHSVNMAPS GIHMQYHVPH
QGKERRFYPK EVLVSSRPGN
//