GenomeNet

Database: UniProt
Entry: A0A2Y9KCQ9_ENHLU
LinkDB: A0A2Y9KCQ9_ENHLU
Original site: A0A2Y9KCQ9_ENHLU 
ID   A0A2Y9KCQ9_ENHLU        Unreviewed;       785 AA.
AC   A0A2Y9KCQ9;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Paraplegin isoform X1 {ECO:0000313|RefSeq:XP_022367190.1};
GN   Name=LOC111152823 {ECO:0000313|RefSeq:XP_022367190.1};
OS   Enhydra lutris kenyoni (northern sea otter).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Lutrinae; Enhydra.
OX   NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022367190.1};
RN   [1] {ECO:0000313|RefSeq:XP_022367190.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022367190.1};
RG   RefSeq;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC       family. {ECO:0000256|ARBA:ARBA00010044}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the AAA ATPase
CC       family. {ECO:0000256|ARBA:ARBA00010550}.
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   RefSeq; XP_022367190.1; XM_022511482.1.
DR   AlphaFoldDB; A0A2Y9KCQ9; -.
DR   STRING; 391180.A0A2Y9KCQ9; -.
DR   KEGG; elk:111152823; -.
DR   OrthoDB; 9585at2759; -.
DR   Proteomes; UP000248482; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd19501; RecA-like_FtsH; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.1690.20; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.20.58.760; Peptidase M41; 1.
DR   HAMAP; MF_01458; FtsH; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR005936; FtsH.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011546; Pept_M41_FtsH_extracell.
DR   InterPro; IPR000642; Peptidase_M41.
DR   InterPro; IPR037219; Peptidase_M41-like.
DR   NCBIfam; TIGR01241; FtsH_fam; 1.
DR   PANTHER; PTHR43655; ATP-DEPENDENT PROTEASE; 1.
DR   PANTHER; PTHR43655:SF8; PARAPLEGIN; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   Pfam; PF06480; FtsH_ext; 1.
DR   Pfam; PF01434; Peptidase_M41; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF140990; FtsH protease domain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..785
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015905306"
FT   TRANSMEM        145..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        250..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          341..481
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          103..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          748..785
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          212..239
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        106..134
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        762..776
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   785 AA;  87028 MW;  86D628676450F390 CRC64;
     MASALLLLRA LCRGRAAGSA PVRGRCLRWS LGLAAGTGRR CWHFVHRPPT RLVGARGHAK
     QTLQLHRLTP AFGGFSGLLL EQHLLQNPVR LWRLLGATRY FNTSTPKQKT KDKDRSKGRT
     PEDDEEERRR REREDQMYRE RLRTLFVIAV IMSLLNALST SGGNISWNDF VHEMLAKGEV
     QRVQVVPESD VVEVYLHPGA VVFGRPRLAL MYRMQVANID RFEEKLRAAE DALNIEGKDR
     IPVSYKRTGF FGNALYALGM TAVGLAILWY VFRLAGMTGR EGGLSAFNQL KMARFTIVDG
     KMGKGVSFKD VAGMHEAKLE VREFVDYLKS PERFLQLGAK VPKGALLLGP PGCGKTLLAK
     AVATEAQVPF LAMAGPEFVE VIGGLGAARV RSLFKEARAR APCIVYIDEI DAVGKKRSTT
     MSGFSNTEEE QTLNQLLVEM DGMGTTDHVI VLASTNRADV LDNALLRPGR LDRHIFIDLP
     TLQERREIFE QHLKSLKLTQ ASSFYSRRLA ELTPGFSGAD IANVCNEAAL HAAREGHASV
     HTLNFECAVE RVIAGTAKKS QILSKEEQKV VAFHESGHAL VGWLLEHTEA VMKVSIAPRT
     NAALGFAQML PRDQHLFTKE QLFERMCMAL GGRASENISF NKVTSGAQDD LRKVTRIAYS
     MVRQFGMAPS IGPVSFPEAQ EGLAGVGQRP FSRGLQEMMD HEAKLLVAKA YRHTEQVLQD
     NLDKLQALAN ALLEKEVINY EDIEALIGPP PHGPKKMIAP QRWSEAETEK QDPGEEEAPQ
     QPPPP
//
DBGET integrated database retrieval system