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}.
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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
//