ID U3KF21_FICAL Unreviewed; 1520 AA.
AC U3KF21;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Ubiquitin specific peptidase 19 {ECO:0000313|Ensembl:ENSFALP00000013625.2};
GN Name=USP19 {ECO:0000313|Ensembl:ENSFALP00000013625.2};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000013625.2, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000013625.2, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000013625.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR STRING; 59894.ENSFALP00000013625; -.
DR Ensembl; ENSFALT00000013681.2; ENSFALP00000013625.2; ENSFALG00000013039.2.
DR eggNOG; KOG1870; Eukaryota.
DR GeneTree; ENSGT00940000159085; -.
DR HOGENOM; CLU_001060_8_1_1; -.
DR Proteomes; UP000016665; Chromosome 12.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:Ensembl.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:Ensembl.
DR GO; GO:0051879; F:Hsp90 protein binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR GO; GO:1900037; P:regulation of cellular response to hypoxia; IEA:Ensembl.
DR GO; GO:1904292; P:regulation of ERAD pathway; IEA:Ensembl.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:Ensembl.
DR CDD; cd06466; p23_CS_SGT1_like; 1.
DR CDD; cd06463; p23_like; 1.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 2.60.40.790; -; 2.
DR Gene3D; 6.10.140.2220; -; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR002893; Znf_MYND.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF74; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 19; 1.
DR Pfam; PF04969; CS; 2.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF16602; USP19_linker; 1.
DR Pfam; PF01753; zf-MYND; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF144232; HIT/MYND zinc finger-like; 1.
DR SUPFAM; SSF49764; HSP20-like chaperones; 2.
DR PROSITE; PS51203; CS; 2.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000016665};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00134}.
FT DOMAIN 54..143
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
FT DOMAIN 376..478
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
FT DOMAIN 593..1443
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 887..929
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS50865"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1006..1034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1114..1136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1446..1520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1485..1520
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1520 AA; 167828 MW; 7E9F36C56D71C2D8 CRC64;
MSSSTNAPGQ RRASRGLDDA TNKKKQKDRA NQESKEVSRP ELEQAETAQE KDSEEELLLD
WKQNADEIII KLNLGSGALK AEDVRADFTD TDCVVKLPDG RQWSCQFYEE IEGSCSKIQC
KKGNFLQLVL QKKIPLHNWA SLLKKRKDGS KEPAKGVVCW ENGKEKAASA ELTPAEPRAE
GTEPPRSRRE PSNPKRAPGR SEALGGKSPA SPGTQSGPSA KRAVYLKVAP TEEEPSARVT
GSTEPGKGHS GRAGSRRNGR ASQADAPVAL ADLALPLEKA VVLAKETVPV EMPPLSATTE
VFPHRVATCV EKRVLQPGSP AEALLSRDCL PILGESSKAI PLATPPVGRD VEKRDWSKDE
VALEAAADEP EPFVSLTFVK NDSYEKGNDL VVVHVYVKEI HKETSKVLFR EQDFTLVFQT
SDTNFLRLHP GCGPHTVFRW QVKLRNLIEP DQCTYNFTVS RIDVCLKKRQ SQRWGGLEAP
ATRGAVGGAK VAMPTGPTPL DKNPPGSNQH PLSSKEEART SDKEKPRVED GALDGVAART
APEHLAVKQE PHIPSPKPTC MVPPMTHSPV SAESVEDDED EDEKKKVCLP GFTGLVNLGN
TCFMNSVIQS LSNTRELRDY FHDRSFESEI NYNNPLGTGG RLAIGFAMLL RALWKGTHHA
FQPSKLKAIV ASKASQFTGY AQHDAQEFMA FLLDGLHEDL NRIQNKPYTE TVDSDGRPDE
VVAEEAWQRH KMRNDSFIVD LFQGQYKSKL VCPVCSKVSI TFDPFLYLPV PLPQKQKVLT
VYYFAKEPHK KPIKFLVSIS KENSSAMEVL DSVAHSVRVK PENLRLAEVV KNHFHRMFLP
SNSLDTVSPT DLLLCFEVLS PELAKERVVE LQVQQRPQVP SGPVAKCAAC QKKQLPEDEK
LKRCTRCYRV GYCNVACQKT HWPDHKASCR PENIGFPFLI SVPESRLTYA RLAQLLEGYA
RYSVSVFQPP FQLGRMSPEQ GLQPLHSDKL EPLAKSSCAA ATSASELGDG DRISSLPQEP
PLSPAVPELQ PEMGDTTTVR SKVLTARSSL LSLDSGFSEH MESQGDSCCE KEPSYERALK
PEAAIPGYQH TPDSLSARAT QFYITKIDAA NREQKLEDKG EPEPCKAPPS SLTASGRVVG
LPGRGARGRL AQGSRSKVLT ARSSLLSLDS GFSEHMESQG DSCCEKEPSY ERALKPEAAI
PGYQHTPDSL SARATQFYIT KIDAANREQK LEDKGDTPLD LTDDCSLALV WQNNERLKEF
VLVESKELEC VEDPGSASEA ARAGHFTLEQ CLNLFTKPEV LAPEEAWYCP KCKQHREASK
QLMLWRLPNV LIIQLKRFSF RSFIWRDKIN DMVDFPVRSL DLSKFCIGRK GEQQLPMYDL
YAVINHYGGM IGGHYTAYAR LPNDKNSQRS DVGWRLFDDS TVTTVDESQV VTRYAYVLFY
RRRNSPVERP LPGHPSDHRA ERTPSAEAAA SQGLPPVAFG SSLAPEGAPP PPPPPPPPPP
PPPPPPPPPP PPPPPPPPPP
//
