ID A0A1S3ERS1_DIPOR Unreviewed; 965 AA.
AC A0A1S3ERS1;
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 X6 {ECO:0000313|RefSeq:XP_012867101.1};
GN Name=Atxn2l {ECO:0000313|RefSeq:XP_012867101.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012867101.1};
RN [1] {ECO:0000313|RefSeq:XP_012867101.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012867101.1};
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_012867101.1; XM_013011647.1.
DR AlphaFoldDB; A0A1S3ERS1; -.
DR GeneID; 105982155; -.
DR CTD; 11273; -.
DR OrthoDB; 4269134at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
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 PANTHER; PTHR12854; ATAXIN 2-RELATED; 1.
DR PANTHER; PTHR12854:SF8; ATAXIN-2-LIKE PROTEIN; 1.
DR Pfam; PF06741; LsmAD; 1.
DR Pfam; PF07145; PAM2; 1.
DR Pfam; PF14438; SM-ATX; 1.
DR SMART; SM01272; LsmAD; 1.
DR PROSITE; PS52002; SM; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000081671}.
FT DOMAIN 25..102
FT /note="Sm"
FT /evidence="ECO:0000259|PROSITE:PS52002"
FT REGION 220..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 767..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..367
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..488
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..820
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..837
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 965 AA; 102460 MW; EE8367388F32F0D9 CRC64;
MERGQSTGKG PPQSPVFEGV YNNSRMLHFL TAVVGSTCDV KVKNGTTYEG IFKTLSSKFE
LAVDAVHRKA SEPAGGPRRE DIVDTMVFKP SDVMLVHFRN VDFNYATKDK FTDSAIAMNS
KVNGEHKEKV LQRWEGGDSN SDDYDLESDM SNGWDPNEMF KFNEENYGVK TTYDSSLSSY
TVPLEKDNSE EFRQRELRAA QLAREIESSP QYRLRIAMEN EDGRTEEEKH SAVQRQGSGR
ESPSLASREG KYIPLPQRVR EGPRGGVRCS SSRGGRPGLS SLPPRGPHHL DNSSPGPGSE
TRGINGGPSR MSPKAQRPLR GAKTLSSPNS RPSGEASVPP PAAVGRMYPP RSPKSAVPAP
ISAPCPEPPI GSAVATSAAS IPVTSAVDPG AGSITPASPK ISLAPTDVKE LPPKEPGRTL
EPQDLARIAG KVSGLQNEQK RFQLEELRKF GAQFKLQPPS SPETSLDPFS PRILKEEAKG
KEKEVDGLLT SESMGSPVSS KTESVSDKED KAPLASAGGA EGSEQPPPPC PSQTGSPPVG
LIKGDDKDEG PVAEQVKKST LNPNAKEFNP TKPLLSVNKS TSTPTSPGPR THSTPSIPVL
TAGQSGLYSP QYISYIPQIH MGPAVQAPQM YPYPVSNSVP GQQGKYRGAK GSLPPQRSDQ
HQPASAPPMM QAAAAAGPPL VAATPYSSYI PYNPQQFPGQ PAMMQPMAHY PSQPVFAPML
QSNQRMLTSG SHPPAIVSSS TPQYPSAEQP TPQALYATVH QSYPHHATQL HAHQPQPATT
PTGSQPQSQH AAPSPVQHQA GQAPHLGSGQ PQQNLYHPGA LTGTPPSLPP GPSAQSPQSS
FPQPAAVYAI HPHQQLPHGF TNMAHVTQAH VQTGVTAAPP PHPGAPHPPQ VMLLHPTQGH
GGPPQGAVPP SGVPALSAST PSPYPYIGHP QGEQPGQAPG FPGGADDRIL QSHPSQQLPF
HPPGN
//