ID A0A0Q3T0S3_AMAAE Unreviewed; 1150 AA.
AC A0A0Q3T0S3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=SUMO-specific isopeptidase USPL1 {ECO:0000313|EMBL:KQK74110.1};
GN ORFNames=AAES_160811 {ECO:0000313|EMBL:KQK74110.1};
OS Amazona aestiva (Blue-fronted Amazon parrot).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX NCBI_TaxID=12930 {ECO:0000313|EMBL:KQK74110.1, ECO:0000313|Proteomes:UP000051836};
RN [1] {ECO:0000313|EMBL:KQK74110.1, ECO:0000313|Proteomes:UP000051836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FVVF132 {ECO:0000313|EMBL:KQK74110.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQK74110.1}.
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DR EMBL; LMAW01003089; KQK74110.1; -; Genomic_DNA.
DR STRING; 12930.A0A0Q3T0S3; -.
DR Proteomes; UP000051836; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008047; F:enzyme activator activity; IEA:InterPro.
DR GO; GO:0032183; F:SUMO binding; IEA:InterPro.
DR GO; GO:0030576; P:Cajal body organization; IEA:InterPro.
DR GO; GO:0019370; P:leukotriene biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.550; Membrane associated eicosanoid/glutathione metabolism-like domain; 1.
DR InterPro; IPR001446; 5_LipOase_AP.
DR InterPro; IPR029388; DUF4650.
DR InterPro; IPR023352; MAPEG-like_dom_sf.
DR InterPro; IPR001129; Membr-assoc_MAPEG.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR028890; Peptidase_C98.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR033505; USPL1.
DR PANTHER; PTHR15294; RETINOVIN-RELATED; 1.
DR PANTHER; PTHR15294:SF3; SUMO-SPECIFIC ISOPEPTIDASE USPL1; 1.
DR Pfam; PF15509; DUF4650; 1.
DR Pfam; PF01124; MAPEG; 1.
DR Pfam; PF15499; Peptidase_C98; 2.
DR PRINTS; PR00488; 5LPOXGNASEAP.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF161084; MAPEG domain-like; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Leukotriene biosynthesis {ECO:0000256|ARBA:ARBA00022751};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000051836};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1056..1082
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1103..1125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 227..463
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 179..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 774..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..826
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1150 AA; 127209 MW; 65E36A4B0D4EF10B CRC64;
MMDTQKTTNG LQVIGEGTGI GKSTLHMNCN PVETAAHEHC PVCQEKGQIH VLRTYRINFQ
ESIFLCANPQ CIYPLGYKPL NSIITSADSE NHQVPSTDKK RKLCGISDFS PVESYPKKAR
TNNGANGVHS INTDPVVKSY QNGLCLPKSS LHDVLQDDQQ KPSISVEVCT QKVDFETTTN
TKNSKESPSN ASSPGAQLLP NSELSSTTSE ILLKGDKGST NNTDLCLQWR NVHNLCWLDC
ILSALVHLET LKFPLAEEYN DGKCLVQELL TKYNQATVLL NTCKRSRVKG KKESPVFALP
LLLQLDQQAE KLFLHSFSWK FECVCCGYKY QNRLRKTLTT FTNIIPDWHP LNAVHVGPCN
NCSDRSQRRQ MILETVPSIL MLHFVEGLPH NNLENYSFQF EENTYEITSV VQYQTDKQHF
ITWSLNSDGS WLECDDLKGP YCERHSTFEV PPSEIHIAVW EKKTSHVPEE PSSQFESRNI
EDFPFNNVQS NSAVLHCGFD NTVDKTPAEH LKEDSARNPS EKQQQVAKDE SIVPHDLATL
MLEEIQVNSE GKSLPNGQVV GNNLVEMGTP QKQELDLLPN TPCTGRFAGT RLAMSNKCML
YEDSSICLPL DKFNPTNVTP PVPKTHHPDP SDSLGQRTDG RTNLHGGLNS ELQLNKKLSP
VENIQKSPDF KDASKTVMNS QVAGSAAASK SFQPSHKDQK RGFVGSWVKK LLNKNTSFMP
SSASALKNER SCKTPSMQKI SEVRLPVKGA SNFGGFQSRG TSKTTEALKS VVPQSNNTHP
LSTFKGFSQN TRLPTASHTT TECPTWTKSG STSGTSGKAT QFHSHSHNSG KAEESDTDQT
KKLRLKLLKK LNAXKKKLAS LDRLAVEQVK HGKLVNGDVG TAPQTESHND SELLQSFLRE
LQCQIDAADN ESEFSTNSVS GCTSNDEILA ELLSPASTVA SLEAPKSEDE CMYMEMVDSS
VPTTASDXKT SVPHAAVTSE DHNYYSPVKE SNSELHTVSK SSVKKLALES PTREDILEDL
FSISAPSSMA GDIDLPHFDE TLFETCQNCG XAYPTFLAVL WCAGLLCSPA PAAFAGLMYL
FVRQKYFVGY LGERTQSTPG HLFGKRIILF LFLMSVAGIL NYYLIFFFGS DFEVHIKTIT
SAISPLLLIP
//
