ID D7MNY6_ARALL Unreviewed; 1006 AA.
AC D7MNY6;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Reticulon-like protein {ECO:0000256|RuleBase:RU363132};
GN ORFNames=ARALYDRAFT_332090 {ECO:0000313|EMBL:EFH40802.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000256|ARBA:ARBA00001512};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC Evidence={ECO:0000256|ARBA:ARBA00001482};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363132}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC ECO:0000256|RuleBase:RU363132}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
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; GL348720; EFH40802.1; -; Genomic_DNA.
DR RefSeq; XP_002864543.1; XM_002864497.1.
DR AlphaFoldDB; D7MNY6; -.
DR STRING; 81972.D7MNY6; -.
DR EnsemblPlants; fgenesh1_pm.C_scaffold_8001433; fgenesh1_pm.C_scaffold_8001433; fgenesh1_pm.C_scaffold_8001433.
DR Gramene; fgenesh1_pm.C_scaffold_8001433; fgenesh1_pm.C_scaffold_8001433; fgenesh1_pm.C_scaffold_8001433.
DR eggNOG; KOG0323; Eukaryota.
DR HOGENOM; CLU_298669_0_0_1; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IEA:InterPro.
DR CDD; cd17729; BRCT_CTDP1; 1.
DR CDD; cd07521; HAD_FCP1-like; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR039189; Fcp1.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR011947; FCP1_euk.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR003388; Reticulon.
DR NCBIfam; TIGR02250; FCP1_euk; 1.
DR PANTHER; PTHR23081; RNA POLYMERASE II CTD PHOSPHATASE; 1.
DR PANTHER; PTHR23081:SF36; RNA POLYMERASE II SUBUNIT A C-TERMINAL DOMAIN PHOSPHATASE; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF03031; NIF; 1.
DR Pfam; PF02453; Reticulon; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM00577; CPDc; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS50969; FCP1; 1.
DR PROSITE; PS50845; RETICULON; 1.
PE 4: Predicted;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU363132}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363132};
KW Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU363132};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU363132}.
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363132"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363132"
FT TRANSMEM 439..460
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363132"
FT DOMAIN 279..379
FT /note="Reticulon"
FT /evidence="ECO:0000259|PROSITE:PS50845"
FT DOMAIN 688..868
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT DOMAIN 902..994
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..242
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..622
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1006 AA; 114593 MW; 3AED61D61F1E4FD8 CRC64;
MDPSINSSRR RRIGGTAGSV CETRMQSDDE VSNNAIVLHV TNEDKTSSTK QMSLKEEALG
VNGKRRTWKS RAFDVKNPST LEIVRTNSLK VTRPRSIGTP PMTPRRSLSS NDSNEKSPSL
SVAAKKARSD SVEGIEKTTP GRVKKTRSEL CTTIVKAGEF DSVALRKVSS LPVPNSEKSD
KKTEHVVDVP KEETINENSK IPEEVKEFGV CQEMIVSAKS NEDEQINDGD HEEDDEEEKE
EEVEKKSVDV KEMNVAKENR VGVEIKKLSQ FQNRTSPSPS SILMWRDVSR STLVFGFGTF
LIISSSYAND LNFSFISVVA YMGLIYLGLM FVLKSLIHRG MVEEERHKVV GVREEDVKRM
LRLIMPYLNE SLHQLRALFS GDPSTTLKMG VVLFVLARCG SSITLWNLAK FGNFWMRRFR
DAWESCNHKK AVSLALFTLV WNLSSVTARV WAAFMLLVAF RYYQHKMIWT TDQADDDDDE
NVVDEEEEEE EEKEQLGLLM GPKRALLHKL ISFREITNRR EVESFTFSLS RLHTVAASPL
FPLKTQNHDF EVLSPQANKF KMSVASDSPV HSSSSSDDLA AFLDAELDSA SDASSGPSEE
EEEAEDDEES GLKRRKLEHL ETVDEEEIEE ASSSKGECQH PGSFGNMCFV CGQKLEETGV
SFRYIHKEMR LNEDEISRLR DSDSRFLQRQ RKLYLVLDLD HTLLNSTVLR DLKPEEEYLK
SHTHSLQEPF DFLLISDVSG GSLFMLEFMH MMTKLRPFVH SFLKEASEMF VMYIYTMGDR
AYARQMAKLL DPRGEYFGDR IISRDDGTVR HQKSLDVVLG QESAVLILDD TENAWPNHKD
NLIVIERYHF FASSCRQFDH KYKSLSELKS DESEPDGALA TVLKNVDEDI SNRDVRSMLK
QVRKEVLKGC KVVFSRVFPT KAKPEDHPLW KMAEELGATC ATEVDASVTH VVAMDVGTEK
ARWAVREKKY VVHRGWIDAA NYLWKKQPEE KFSLEQLKKQ QVAEEE
//
