ID Q7ZYF3_XENLA Unreviewed; 762 AA.
AC Q7ZYF3;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 122.
DE SubName: Full=Calpain 13 L homeolog {ECO:0000313|RefSeq:NP_001079488.1};
DE SubName: Full=MGC53127 protein {ECO:0000313|EMBL:AAH43810.1};
GN Name=capn13.L {ECO:0000313|RefSeq:NP_001079488.1,
GN ECO:0000313|Xenbase:XB-GENE-6045553};
GN Synonyms=capn11 {ECO:0000313|RefSeq:NP_001079488.1}, capn13
GN {ECO:0000313|RefSeq:NP_001079488.1,
GN ECO:0000313|Xenbase:XB-GENE-6045553};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|EMBL:AAH43810.1};
RN [1] {ECO:0000313|RefSeq:NP_001079488.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12454917; DOI=10.1002/dvdy.10174;
RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA Richardson P.;
RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT initiative.";
RL Dev. Dyn. 225:384-391(2002).
RN [2] {ECO:0000313|EMBL:AAH43810.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000313|EMBL:AAH43810.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:NP_001079488.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase C2 family.
CC {ECO:0000256|ARBA:ARBA00007623}.
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 EMBL; BC043810; AAH43810.1; -; mRNA.
DR RefSeq; NP_001079488.1; NM_001086019.1.
DR MEROPS; C02.020; -.
DR DNASU; 379175; -.
DR GeneID; 379175; -.
DR KEGG; xla:379175; -.
DR AGR; Xenbase:XB-GENE-6045553; -.
DR CTD; 379175; -.
DR Xenbase; XB-GENE-6045553; capn13.L.
DR OrthoDB; 142935at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 379175; Expressed in stomach and 11 other cell types or tissues.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00044; CysPc; 1.
DR CDD; cd16195; EFh_PEF_CAPN13_14; 1.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR InterPro; IPR022684; Calpain_cysteine_protease.
DR InterPro; IPR022682; Calpain_domain_III.
DR InterPro; IPR022683; Calpain_III.
DR InterPro; IPR036213; Calpain_III_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR PANTHER; PTHR10183; CALPAIN; 1.
DR PANTHER; PTHR10183:SF333; CALPAIN-13; 1.
DR Pfam; PF01067; Calpain_III; 1.
DR Pfam; PF00648; Peptidase_C2; 1.
DR PRINTS; PR00704; CALPAIN.
DR SMART; SM00720; calpain_III; 1.
DR SMART; SM00230; CysPc; 1.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF49758; Calpain large subunit, middle domain (domain III); 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 2: Evidence at transcript level;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00239};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU00239}; Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807, ECO:0000256|PROSITE-
KW ProRule:PRU00239}.
FT DOMAIN 47..343
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT DOMAIN 664..699
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 508..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..540
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 105
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 261
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 285
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 762 AA; 87294 MW; 3C9CE016E2D3D9F3 CRC64;
MPMPGVYQKI AEGQQVQRRI GTVENPKKFK GQDFDSIRET CYSRRQLFED ETFPAHVNSI
GQKVLPKDQL LSVQWERPKE IQRDARLLVD GASIFDIVQG QIGDCWVLSA VGALTLHQKF
LDNVIPKDQE FNYKYAGVFH FRFWQFGEWV DVVIDDRLPM LNGKYLSVQP RSGNEFWPGL
LEKAYAKLHG SYQNLHWGYI SEALVDFSGG VQVEFDLMRP PQDLRDIVIA AAKTGSLLGC
ITPGNKRSGN PELKNGLVQG HAYTVTDATK VEYKNGTEDL IRIWNPWGKG EWNGRWSDNS
PQWDQVRADI RHKLNVQKND GEFWISCQDF LQNFSFVSIC NHTPAYFDFE NPKRAWQELT
YFDRWVKGST AAGCSTSEDL WRNPQFVISV SDSEGMNRGY NVTVALMQSL ENQNKYNQEW
MGIGFAFCKV ASKGVKSLSQ QNYSPNQAVD VINTEIQISR EITRSFRAPP GTYVVIPFTQ
SKGLESEFLL RIFLKTKEID KFQDTTLVPR EGNQTYPSDS RLRYQDTKPK PRDEKQIFNP
NEIRARNQSN SSLPREENQY QYASDAGLSE FSSSLSMNSQ IPKAVLKKYQ NDGYEKVFIR
YCNKSSELYA EQLQKLLNEV LIKDQTFNAS RGDFTLDACR GILMLMDLNA NGRLNLQEFE
RLWKRLSMCK DIFRSIDLNQ TGFVDASGLR KAAQLTGLPI SNAVINVMVL RYANSLEKLN
FADFVCCIIR LETVTKVFKN LSKDGRGVYL SGEEWMQIIM SS
//
