ID A0A1S3JXF4_LINUN Unreviewed; 326 AA.
AC A0A1S3JXF4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Cathepsin L1-like {ECO:0000313|RefSeq:XP_013415058.1};
GN Name=LOC106176992 {ECO:0000313|RefSeq:XP_013415058.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013415058.1};
RN [1] {ECO:0000313|RefSeq:XP_013415058.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013415058.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase C1 family.
CC {ECO:0000256|ARBA:ARBA00008455}.
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DR RefSeq; XP_013415058.1; XM_013559604.1.
DR AlphaFoldDB; A0A1S3JXF4; -.
DR STRING; 7574.A0A1S3JXF4; -.
DR EnsemblMetazoa; XM_013559604.1; XP_013415058.1; LOC106176992.
DR GeneID; 106176992; -.
DR KEGG; lak:106176992; -.
DR InParanoid; A0A1S3JXF4; -.
DR OrthoDB; 5472948at2759; -.
DR Proteomes; UP000085678; Unplaced.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02248; Peptidase_C1A; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025661; Pept_asp_AS.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR013128; Peptidase_C1A.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR InterPro; IPR013201; Prot_inhib_I29.
DR PANTHER; PTHR12411:SF971; CATHEPSIN L-RELATED; 1.
DR PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00848; Inhibitor_I29; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW Signal {ECO:0000256|SAM:SignalP};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..326
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012729539"
FT DOMAIN 26..86
FT /note="Cathepsin propeptide inhibitor"
FT /evidence="ECO:0000259|SMART:SM00848"
FT DOMAIN 115..326
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
SQ SEQUENCE 326 AA; 36436 MW; 0FCE85AAAAD4A7CC CRC64;
MKYLVLLACA SVALACKCNQ KLDDEWEVYK KFHNKVYETP TEDCYRRNLW EDSVQWVAKH
NREYDMGVHT YWVGINQFSD MTQQERVRKM NGAVMPQNLT YDGMEWFQEP LNVELPSTVD
WRQKGAVTPV KNQGGCGSCW AFSATGTMEG QSYLRKHKKV SISEQQLVDC DKRDGGCNGG
WPYVAIQYVA KNGGIDTETA YRYTGKDGSC HFSKSGVGYT TSGVVHVPAS ESSLQSAVAT
VGPISVCIDA SHRSFGSYKG GVYNEPACTH RTDHCVLAVG YGTMSGQAYW LVKNSWSTRW
GVQGYIYMSR NKGNQCAIAS YGTYSK
//
