CAN14_HUMAN
ID CAN14_HUMAN Reviewed; 684 AA.
AC A8MX76; B3KRU9;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Calpain-14;
DE EC=3.4.22.-;
DE AltName: Full=Calcium-activated neutral proteinase 14;
DE Short=CANP 14;
GN Name=CAPN14;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP IDENTIFICATION, AND LACK OF TISSUE SPECIFICITY.
RX PubMed=11675017; DOI=10.1016/s0378-1119(01)00599-6;
RA Dear T.N., Boehm T.;
RT "Identification and characterization of two novel calpain large subunit
RT genes.";
RL Gene 274:245-252(2001).
CC -!- FUNCTION: Calcium-regulated non-lysosomal thiol-protease.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A8MX76-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A8MX76-2; Sequence=VSP_034268, VSP_034269;
CC -!- TISSUE SPECIFICITY: Not expressed in tissues tested.
CC -!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
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DR EMBL; AK092257; BAG52511.1; -; mRNA.
DR EMBL; AC015980; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS46254.1; -. [A8MX76-1]
DR RefSeq; NP_001138594.1; NM_001145122.1. [A8MX76-1]
DR RefSeq; NP_001308199.1; NM_001321270.1. [A8MX76-2]
DR RefSeq; XP_011531165.1; XM_011532863.2. [A8MX76-1]
DR RefSeq; XP_011531166.1; XM_011532864.2. [A8MX76-1]
DR RefSeq; XP_011531167.1; XM_011532865.1. [A8MX76-1]
DR RefSeq; XP_011531168.1; XM_011532866.2. [A8MX76-2]
DR AlphaFoldDB; A8MX76; -.
DR SMR; A8MX76; -.
DR STRING; 9606.ENSP00000385247; -.
DR MEROPS; C02.021; -.
DR iPTMnet; A8MX76; -.
DR PhosphoSitePlus; A8MX76; -.
DR BioMuta; CAPN14; -.
DR MassIVE; A8MX76; -.
DR MaxQB; A8MX76; -.
DR PaxDb; A8MX76; -.
DR PeptideAtlas; A8MX76; -.
DR PRIDE; A8MX76; -.
DR ProteomicsDB; 2300; -. [A8MX76-1]
DR ProteomicsDB; 2301; -. [A8MX76-2]
DR Antibodypedia; 51640; 46 antibodies from 9 providers.
DR DNASU; 440854; -.
DR Ensembl; ENST00000403897.4; ENSP00000385247.3; ENSG00000214711.10. [A8MX76-1]
DR GeneID; 440854; -.
DR KEGG; hsa:440854; -.
DR MANE-Select; ENST00000403897.4; ENSP00000385247.3; NM_001145122.2; NP_001138594.1.
DR UCSC; uc010yms.3; human. [A8MX76-1]
DR CTD; 440854; -.
DR DisGeNET; 440854; -.
DR GeneCards; CAPN14; -.
DR HGNC; HGNC:16664; CAPN14.
DR HPA; ENSG00000214711; Tissue enriched (esophagus).
DR MIM; 610229; gene.
DR neXtProt; NX_A8MX76; -.
DR OpenTargets; ENSG00000214711; -.
DR PharmGKB; PA134888839; -.
DR VEuPathDB; HostDB:ENSG00000214711; -.
DR eggNOG; KOG0045; Eukaryota.
DR GeneTree; ENSGT00940000160421; -.
DR HOGENOM; CLU_010982_0_3_1; -.
DR InParanoid; A8MX76; -.
DR OMA; TMSIQEF; -.
DR PhylomeDB; A8MX76; -.
DR TreeFam; TF314748; -.
DR PathwayCommons; A8MX76; -.
DR Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
DR BioGRID-ORCS; 440854; 10 hits in 1065 CRISPR screens.
DR GenomeRNAi; 440854; -.
DR Pharos; A8MX76; Tdark.
DR PRO; PR:A8MX76; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; A8MX76; protein.
DR Bgee; ENSG00000214711; Expressed in lower esophagus mucosa and 76 other tissues.
DR ExpressionAtlas; A8MX76; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd00214; Calpain_III; 1.
DR CDD; cd00044; CysPc; 1.
DR InterPro; IPR033883; C2_III.
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; IPR018247; EF_Hand_1_Ca_BS.
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 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 SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF49758; SSF49758; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 3.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Hydrolase; Metal-binding; Protease;
KW Reference proteome; Repeat; Thiol protease.
FT CHAIN 1..684
FT /note="Calpain-14"
FT /id="PRO_0000341373"
FT DOMAIN 43..336
FT /note="Calpain catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT DOMAIN 557..592
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 586..621
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 651..684
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 337..503
FT /note="Domain III"
FT REGION 504..517
FT /note="Linker"
FT REGION 518..683
FT /note="Domain IV"
FT ACT_SITE 101
FT /evidence="ECO:0000250"
FT ACT_SITE 254
FT /evidence="ECO:0000250"
FT ACT_SITE 278
FT /evidence="ECO:0000250"
FT BINDING 570
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 572
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 574
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 576
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 581
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT VAR_SEQ 1..176
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_034268"
FT VAR_SEQ 177..184
FT /note="LLEKAYAK -> MLASSGSG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_034269"
SQ SEQUENCE 684 AA; 79568 MW; 6627B859E4F375A9 CRC64;
MSLWPPFRCR WKLAPRYSRR ASPQQPQQDF EALLAECLRN GCLFEDTSFP ATLSSIGSGS
LLQKLPPRLQ WKRPPELHSN PQFYFAKAKR LDLCQGIVGD CWFLAALQAL ALHQDILSRV
VPLNQSFTEK YAGIFRFWFW HYGNWVPVVI DDRLPVNEAG QLVFVSSTYK NLFWGALLEK
AYAKLSGSYE DLQSGQVSEA LVDFTGGVTM TINLAEAHGN LWDILIEATY NRTLIGCQTH
SGEKILENGL VEGHAYTLTG IRKVTCKHRP EYLVKLRNPW GKVEWKGDWS DSSSKWELLS
PKEKILLLRK DNDGEFWMTL QDFKTHFVLL VICKLTPGLL SQEAAQKWTY TMREGRWEKR
STAGGQRQLL QDTFWKNPQF LLSVWRPEEG RRSLRPCSVL VSLLQKPRHR CRKRKPLLAI
GFYLYRMNKY HDDQRRLPPE FFQRNTPLSQ PDRFLKEKEV SQELCLEPGT YLIVPCILEA
HQKSEFVLRV FSRKHIFYEI GSNSGVVFSK EIEDQNERQD EFFTKFFEKH PEINAVQLQN
LLNQMTWSSL GSRQPFFSLE ACQGILALLD LNASGTMSIQ EFRDLWKQLK LSQKVFHKQD
RGSGYLNWEQ LHAAMREAGI MLSDDVCQLM LIRYGGPRLQ MDFVSFIHLM LRVENMEDVF
QNLTQDGKGI YLQKPEWMMM ALYS
