CASP_MESAU
ID CASP_MESAU Reviewed; 695 AA.
AC P15156;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Calcium-dependent serine proteinase;
DE Short=CASP;
DE EC=3.4.21.-;
DE Contains:
DE RecName: Full=Calcium-dependent serine proteinase heavy chain;
DE Contains:
DE RecName: Full=Calcium-dependent serine proteinase light chain;
DE Flags: Precursor;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 22-50 AND 446-472.
RC TISSUE=Fibroblast;
RX PubMed=2753140; DOI=10.1016/0014-5793(89)80766-5;
RA Kinoshita H., Sakiyama H., Tokunaga K., Imajoh-Ohmi S., Hamada Y.,
RA Isono K., Sakiyama S.;
RT "Complete primary structure of calcium-dependent serine proteinase capable
RT of degrading extracellular matrix proteins.";
RL FEBS Lett. 250:411-415(1989).
CC -!- FUNCTION: Capable of degrading extracellular matrix proteins. CASP
CC degrades type I and IV collagen and fibronectin in the presence of
CC calcium.
CC -!- SUBUNIT: Heterodimer, consisting of heavy and light chains with
CC disulfide bonds. The heavy chain is expected to be a regulatory subunit
CC and the light chain contains the catalytic site.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate
CC and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; X16160; CAA34286.1; -; mRNA.
DR PIR; S05008; S05008.
DR RefSeq; NP_001268589.1; NM_001281660.1.
DR AlphaFoldDB; P15156; -.
DR SMR; P15156; -.
DR STRING; 10036.XP_005066079.1; -.
DR MEROPS; S01.193; -.
DR GeneID; 101823163; -.
DR CTD; 716; -.
DR eggNOG; KOG3627; Eukaryota.
DR OrthoDB; 156878at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:Ensembl.
DR GO; GO:0006958; P:complement activation, classical pathway; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00033; CCP; 2.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 2.60.120.290; -; 2.
DR InterPro; IPR035708; Complement_C1s_subcomponent.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24255:SF18; PTHR24255:SF18; 1.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF00084; Sushi; 2.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00032; CCP; 2.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF49854; SSF49854; 2.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF57535; SSF57535; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS50923; SUSHI; 2.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; EGF-like domain;
KW Extracellular matrix; Glycoprotein; Hydrolase; Hydroxylation; Protease;
KW Reference proteome; Repeat; Secreted; Serine protease; Signal; Sushi.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:2753140"
FT CHAIN 22..695
FT /note="Calcium-dependent serine proteinase"
FT /id="PRO_0000027589"
FT CHAIN 22..444
FT /note="Calcium-dependent serine proteinase heavy chain"
FT /id="PRO_0000027590"
FT CHAIN 445..695
FT /note="Calcium-dependent serine proteinase light chain"
FT /id="PRO_0000027591"
FT DOMAIN 22..136
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 137..178
FT /note="EGF-like; calcium-binding"
FT /evidence="ECO:0000255"
FT DOMAIN 181..296
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 298..362
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 363..430
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 445..687
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 482
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 536
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 638
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT MOD_RES 155
FT /note="(3R)-3-hydroxyasparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 71..89
FT /evidence="ECO:0000250"
FT DISULFID 141..153
FT /evidence="ECO:0000250"
FT DISULFID 149..162
FT /evidence="ECO:0000250"
FT DISULFID 164..177
FT /evidence="ECO:0000250"
FT DISULFID 181..208
FT /evidence="ECO:0000250"
FT DISULFID 240..257
FT /evidence="ECO:0000250"
FT DISULFID 300..347
FT /evidence="ECO:0000250"
FT DISULFID 327..360
FT /evidence="ECO:0000250"
FT DISULFID 365..410
FT /evidence="ECO:0000250"
FT DISULFID 392..428
FT /evidence="ECO:0000250"
FT DISULFID 602..625
FT /evidence="ECO:0000250"
FT DISULFID 634..666
FT /evidence="ECO:0000250"
SQ SEQUENCE 695 AA; 77493 MW; E924F7E6340700D0 CRC64;
MGKSSEAWCI VLFSVFASFS AEPTMHGEIL SPNYPQAYPN EMEKTWDIEV PEGFGVRLYF
THLDMELSEN CEYDSVQIIS GGVEEGRLCG QRTSKNANSP IVEEFQIPYN KLQVIFRSDF
SNEERFTGFA AYYAAIDVNE CTDFTDVPCS HFCNNFIGGY FCSCPPEYFL HDDMRNCGVN
CSGNVFTALI GEISSPNYPN PYPENSRCEY QILLEEGFQV VVTIQREDFD VEPADSQGNC
QDSLLFAAKN RQFGPFCGNG FPGPLTIETH SNTLDIVFQT DLTEQKKGWK LRYHGDPIPC
PKEITANSVW APEKAKYVFK DVVKISCVDG FEAVEGNVGS TFFYSTCQSN GQWSNSRLRC
QPVDCGIPEP IQNGKVDDPE NTLFGSVIHY SCEEPYYYME HAEHGGEYRC AANGSWVNDE
LGIELPKCVP VCGVPTEPFR IQQRIFGGFP AKIQSFPWQV FFEFPRAGGA LIGEHWVLTA
AHVVEGNSDP SMYVGSTSVR MENLANVQKL TTDRVIIHPG WKPGDDLSTR TNFDNDIALV
RLKDPVKMGP TVSPICLPGT SSEYEPSEGD LGLISGWGRT ERRNIVIQLR GAKLPVTSLE
KCRQVKEENP KARADDYVFT SNMICAGEKG VDSCQGDSGG AFALPVPNVR DPKFYVAGLV
SWGKKCGTYG IYTKVKNYKD WILQTMQENS VPSQD
