CAN10_HUMAN
ID CAN10_HUMAN Reviewed; 672 AA.
AC Q9HC96; A8MVS7; Q4ZFV1; Q8NCD4; Q96IG4; Q96JI2; Q9HC89; Q9HC90; Q9HC91;
AC Q9HC92; Q9HC93; Q9HC94; Q9HC95;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Calpain-10;
DE EC=3.4.22.-;
DE AltName: Full=Calcium-activated neutral proteinase 10;
DE Short=CANP 10;
GN Name=CAPN10; Synonyms=KIAA1845;
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 [MRNA], ALTERNATIVE SPLICING, VARIANTS THR-200;
RP HIS-202; VAL-341; ALA-504; SER-529; ASN-613 AND VAL-666, AND INVOLVEMENT IN
RP SUSCEPTIBILITY TO NIDDM1.
RX PubMed=11017071; DOI=10.1038/79876;
RA Horikawa Y., Oda N., Cox N.J., Li X., Orho-Melander M., Hara M.,
RA Hinokio Y., Lindner T.H., Mashima H., Schwarz P.E.H., del Bosque-Plata L.,
RA Horikawa Y., Oda Y., Yoshiuchi I., Colilla S., Polonsky K.S., Wei S.,
RA Concannon P., Iwasaki N., Schulze J., Baier L.J., Bogardus C., Groop L.,
RA Boerwinkle E., Hanis C.L., Bell G.I.;
RT "Genetic variation in the gene encoding calpain-10 is associated with type
RT 2 diabetes mellitus.";
RL Nat. Genet. 26:163-175(2000).
RN [2]
RP ERRATUM OF PUBMED:11017071.
RA Horikawa Y., Oda N., Cox N.J., Li X., Orho-Melander M., Hara M.,
RA Hinokio Y., Lindner T.H., Mashima H., Schwarz P.E.H., del Bosque-Plata L.,
RA Horikawa Y., Oda Y., Yoshiuchi I., Colilla S., Polonsky K.S., Wei S.,
RA Concannon P., Iwasaki N., Schulze J., Baier L.J., Bogardus C., Groop L.,
RA Boerwinkle E., Hanis C.L., Bell G.I.;
RL Nat. Genet. 26:502-502(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A), AND VARIANT VAL-666.
RC TISSUE=Brain;
RX PubMed=11347906; DOI=10.1093/dnares/8.2.85;
RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 8:85-95(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A), AND VARIANTS ALA-504
RP AND VAL-666.
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A), AND VARIANT VAL-666.
RC TISSUE=Skin, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [8]
RP INVOLVEMENT IN SUSCEPTIBILITY TO NIDDM1.
RX PubMed=16721485; DOI=10.1007/s10038-006-0410-9;
RA Kang E.S., Kim H.J., Nam M., Nam C.M., Ahn C.W., Cha B.S., Lee H.C.;
RT "A novel 111/121 diplotype in the Calpain-10 gene is associated with type 2
RT diabetes.";
RL J. Hum. Genet. 51:629-633(2006).
RN [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17572128; DOI=10.1016/j.ymgme.2007.05.001;
RA Brown A.E., Yeaman S.J., Walker M.;
RT "Targeted suppression of calpain-10 expression impairs insulin-stimulated
RT glucose uptake in cultured primary human skeletal muscle cells.";
RL Mol. Genet. Metab. 91:318-324(2007).
RN [10]
RP VARIANT [LARGE SCALE ANALYSIS] GLY-276.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Calcium-regulated non-lysosomal thiol-protease which
CC catalyzes limited proteolysis of substrates involved in cytoskeletal
CC remodeling and signal transduction. May play a role in insulin-
CC stimulated glucose uptake. {ECO:0000269|PubMed:17572128}.
CC -!- INTERACTION:
CC Q9HC96; Q96G97-4: BSCL2; NbExp=3; IntAct=EBI-3915761, EBI-10178113;
CC Q9HC96; Q16595: FXN; NbExp=3; IntAct=EBI-3915761, EBI-949340;
CC Q9HC96; P04792: HSPB1; NbExp=3; IntAct=EBI-3915761, EBI-352682;
CC Q9HC96; P42858: HTT; NbExp=12; IntAct=EBI-3915761, EBI-466029;
CC Q9HC96; Q99732: LITAF; NbExp=3; IntAct=EBI-3915761, EBI-725647;
CC Q9HC96; P02545-2: LMNA; NbExp=3; IntAct=EBI-3915761, EBI-351953;
CC Q9HC96; P10636: MAPT; NbExp=3; IntAct=EBI-3915761, EBI-366182;
CC Q9HC96; Q9P1N4; NbExp=3; IntAct=EBI-3915761, EBI-25878161;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=A; Synonyms=CAPN10a;
CC IsoId=Q9HC96-1; Sequence=Displayed;
CC Name=B; Synonyms=CAPN10b;
CC IsoId=Q9HC96-2; Sequence=VSP_005232, VSP_005233;
CC Name=C; Synonyms=CAPN10c;
CC IsoId=Q9HC96-3; Sequence=VSP_005234;
CC Name=D; Synonyms=CAPN10d;
CC IsoId=Q9HC96-4; Sequence=VSP_005235, VSP_005236;
CC Name=E; Synonyms=CAPN10e;
CC IsoId=Q9HC96-5; Sequence=VSP_005237, VSP_005238;
CC Name=F; Synonyms=CAPN10f;
CC IsoId=Q9HC96-6; Sequence=VSP_005239, VSP_005240;
CC Name=G; Synonyms=CAPN10g;
CC IsoId=Q9HC96-7; Sequence=VSP_005241, VSP_005242;
CC Name=H; Synonyms=CAPN10h;
CC IsoId=Q9HC96-8; Sequence=VSP_005243;
CC -!- TISSUE SPECIFICITY: Detected in primary skeletal muscle cells (at
CC protein level). Ubiquitous. {ECO:0000269|PubMed:17572128}.
CC -!- DISEASE: Diabetes mellitus, non-insulin-dependent, 1 (NIDDM1)
CC [MIM:601283]: A multifactorial disorder of glucose homeostasis caused
CC by a lack of sensitivity to the body's own insulin. Affected
CC individuals usually have an obese body habitus and manifestations of a
CC metabolic syndrome characterized by diabetes, insulin resistance,
CC hypertension and hypertriglyceridemia. The disease results in long-term
CC complications that affect the eyes, kidneys, nerves, and blood vessels.
CC {ECO:0000269|PubMed:11017071, ECO:0000269|PubMed:16721485}.
CC Note=Disease susceptibility is associated with variants affecting the
CC gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform B]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform D]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform E]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform F]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB47474.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF089088; AAG17966.1; -; mRNA.
DR EMBL; AF089090; AAG17968.1; -; mRNA.
DR EMBL; AF089091; AAG17969.1; -; mRNA.
DR EMBL; AF089092; AAG17970.1; -; mRNA.
DR EMBL; AF089093; AAG17971.1; -; mRNA.
DR EMBL; AF089094; AAG17972.1; -; mRNA.
DR EMBL; AF089095; AAG17973.1; -; mRNA.
DR EMBL; AF089096; AAG17974.1; -; mRNA.
DR EMBL; AB058748; BAB47474.1; ALT_INIT; mRNA.
DR EMBL; AK074807; BAC11220.1; -; mRNA.
DR EMBL; AC124862; AAX88944.1; -; Genomic_DNA.
DR EMBL; BC004260; AAH04260.1; -; mRNA.
DR EMBL; BC007553; AAH07553.2; -; mRNA.
DR CCDS; CCDS33420.1; -. [Q9HC96-3]
DR CCDS; CCDS42838.1; -. [Q9HC96-1]
DR RefSeq; NP_075571.1; NM_023083.3. [Q9HC96-1]
DR RefSeq; NP_075573.2; NM_023085.3. [Q9HC96-3]
DR AlphaFoldDB; Q9HC96; -.
DR SMR; Q9HC96; -.
DR BioGRID; 116305; 34.
DR IntAct; Q9HC96; 13.
DR STRING; 9606.ENSP00000375844; -.
DR MEROPS; C02.018; -.
DR iPTMnet; Q9HC96; -.
DR PhosphoSitePlus; Q9HC96; -.
DR BioMuta; CAPN10; -.
DR DMDM; 317373329; -.
DR MassIVE; Q9HC96; -.
DR PaxDb; Q9HC96; -.
DR PeptideAtlas; Q9HC96; -.
DR PRIDE; Q9HC96; -.
DR ProteomicsDB; 81650; -. [Q9HC96-1]
DR ProteomicsDB; 81651; -. [Q9HC96-2]
DR ProteomicsDB; 81652; -. [Q9HC96-3]
DR ProteomicsDB; 81653; -. [Q9HC96-4]
DR ProteomicsDB; 81654; -. [Q9HC96-5]
DR ProteomicsDB; 81657; -. [Q9HC96-8]
DR Antibodypedia; 1333; 172 antibodies from 24 providers.
DR DNASU; 11132; -.
DR Ensembl; ENST00000270361.15; ENSP00000270361.11; ENSG00000142330.20. [Q9HC96-6]
DR Ensembl; ENST00000270364.11; ENSP00000270364.7; ENSG00000142330.20. [Q9HC96-7]
DR Ensembl; ENST00000352879.8; ENSP00000289381.6; ENSG00000142330.20. [Q9HC96-8]
DR Ensembl; ENST00000354082.8; ENSP00000270362.6; ENSG00000142330.20. [Q9HC96-3]
DR Ensembl; ENST00000357048.8; ENSP00000349556.4; ENSG00000142330.20. [Q9HC96-4]
DR Ensembl; ENST00000391983.7; ENSP00000375843.3; ENSG00000142330.20. [Q9HC96-2]
DR Ensembl; ENST00000391984.7; ENSP00000375844.2; ENSG00000142330.20. [Q9HC96-1]
DR Ensembl; ENST00000416591.5; ENSP00000400144.1; ENSG00000142330.20. [Q9HC96-5]
DR GeneID; 11132; -.
DR KEGG; hsa:11132; -.
DR MANE-Select; ENST00000391984.7; ENSP00000375844.2; NM_023083.4; NP_075571.2.
DR UCSC; uc002vzk.2; human. [Q9HC96-1]
DR CTD; 11132; -.
DR DisGeNET; 11132; -.
DR GeneCards; CAPN10; -.
DR HGNC; HGNC:1477; CAPN10.
DR HPA; ENSG00000142330; Low tissue specificity.
DR MalaCards; CAPN10; -.
DR MIM; 601283; phenotype.
DR MIM; 605286; gene.
DR neXtProt; NX_Q9HC96; -.
DR OpenTargets; ENSG00000142330; -.
DR PharmGKB; PA26058; -.
DR VEuPathDB; HostDB:ENSG00000142330; -.
DR eggNOG; KOG0045; Eukaryota.
DR GeneTree; ENSGT00940000159706; -.
DR HOGENOM; CLU_010982_3_3_1; -.
DR InParanoid; Q9HC96; -.
DR OMA; CYTQDVS; -.
DR OrthoDB; 704215at2759; -.
DR PhylomeDB; Q9HC96; -.
DR TreeFam; TF314748; -.
DR BRENDA; 3.4.22.B30; 2681.
DR PathwayCommons; Q9HC96; -.
DR Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
DR SignaLink; Q9HC96; -.
DR SIGNOR; Q9HC96; -.
DR BioGRID-ORCS; 11132; 19 hits in 1076 CRISPR screens.
DR ChiTaRS; CAPN10; human.
DR GeneWiki; CAPN10; -.
DR GenomeRNAi; 11132; -.
DR Pharos; Q9HC96; Tbio.
DR PRO; PR:Q9HC96; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9HC96; protein.
DR Bgee; ENSG00000142330; Expressed in apex of heart and 126 other tissues.
DR ExpressionAtlas; Q9HC96; baseline and differential.
DR Genevisible; Q9HC96; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR GO; GO:0005739; C:mitochondrion; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; ISS:BHF-UCL.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IMP:BHF-UCL.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISS:BHF-UCL.
DR GO; GO:0000149; F:SNARE binding; ISS:BHF-UCL.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:BHF-UCL.
DR GO; GO:0006921; P:cellular component disassembly involved in execution phase of apoptosis; IC:BHF-UCL.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IMP:BHF-UCL.
DR GO; GO:0046326; P:positive regulation of glucose import; IMP:BHF-UCL.
DR GO; GO:0032024; P:positive regulation of insulin secretion; IMP:BHF-UCL.
DR GO; GO:0032388; P:positive regulation of intracellular transport; ISS:BHF-UCL.
DR GO; GO:2000676; P:positive regulation of type B pancreatic cell apoptotic process; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IMP:BHF-UCL.
DR GO; GO:0097050; P:type B pancreatic cell apoptotic process; IDA:BHF-UCL.
DR CDD; cd00214; Calpain_III; 2.
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; IPR028791; CAPN10.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR PANTHER; PTHR10183:SF30; PTHR10183:SF30; 1.
DR Pfam; PF01067; Calpain_III; 2.
DR Pfam; PF00648; Peptidase_C2; 1.
DR PRINTS; PR00704; CALPAIN.
DR SMART; SM00720; calpain_III; 2.
DR SMART; SM00230; CysPc; 1.
DR SUPFAM; SSF49758; SSF49758; 2.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Diabetes mellitus; Hydrolase; Protease;
KW Reference proteome; Repeat; Thiol protease.
FT CHAIN 1..672
FT /note="Calpain-10"
FT /id="PRO_0000207725"
FT DOMAIN 13..321
FT /note="Calpain catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT REGION 322..494
FT /note="Domain III 1"
FT REGION 513..654
FT /note="Domain III 2"
FT ACT_SITE 73
FT /evidence="ECO:0000250"
FT ACT_SITE 238
FT /evidence="ECO:0000250"
FT ACT_SITE 263
FT /evidence="ECO:0000250"
FT VAR_SEQ 48..581
FT /note="Missing (in isoform H)"
FT /evidence="ECO:0000305"
FT /id="VSP_005243"
FT VAR_SEQ 93..139
FT /note="IPPGQPSWADQEYRGSFTCRIWQFGRWVEVTTDDRLPCLAGRLCFSR -> S
FT CPVQLPADWTCKVQPVWLEFPCLPISCRLRVSSDTSPDSATWGSWK (in isoform
FT G)"
FT /evidence="ECO:0000305"
FT /id="VSP_005241"
FT VAR_SEQ 140..672
FT /note="Missing (in isoform G)"
FT /evidence="ECO:0000305"
FT /id="VSP_005242"
FT VAR_SEQ 154..274
FT /note="VYAKVHGSYEHLWAGQVADALVDLTGGLAERWNLKGVAGSGGQQDRPGRWEH
FT RTCRQLLHLKDQCLISCCVLSPRAGARELGEFHAFIVSDLRELQGQAGQCILLLRIQNP
FT WGRRCWQGLW -> GPWVLRAPVGRAGGGCPGGPDRRPGRKMEPEGRSRKRRPAGQARP
FT LGAQDLSAAAPPEGPVSDQLLRAQPQSRCPGAGGVPCLHCLGPAGAPGSGGPVHPAAAD
FT PEPLGPAVLAGALERGG (in isoform F)"
FT /evidence="ECO:0000305"
FT /id="VSP_005239"
FT VAR_SEQ 275..672
FT /note="Missing (in isoform F)"
FT /evidence="ECO:0000305"
FT /id="VSP_005240"
FT VAR_SEQ 427..444
FT /note="VEKRRVNLPRVLSMPPVA -> GVTLGTTLFPVPSWMWPT (in isoform
FT E)"
FT /evidence="ECO:0000305"
FT /id="VSP_005237"
FT VAR_SEQ 428..582
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_005234"
FT VAR_SEQ 445..672
FT /note="Missing (in isoform E)"
FT /evidence="ECO:0000305"
FT /id="VSP_005238"
FT VAR_SEQ 494..544
FT /note="SAIRAVAKNTTPGAALPAGEWGTVQLRGSWRVGQTAGGSRNFASYPTNPCF
FT -> RALAPAASASLCISTAGPVTPSSTPSASISSRSQRVEGARTHPHCCCRSRC (in
FT isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_005232"
FT VAR_SEQ 494..513
FT /note="SAIRAVAKNTTPGAALPAGE -> RSQRVEGARTHPHCCCRSRC (in
FT isoform D)"
FT /evidence="ECO:0000305"
FT /id="VSP_005235"
FT VAR_SEQ 514..672
FT /note="Missing (in isoform D)"
FT /evidence="ECO:0000305"
FT /id="VSP_005236"
FT VAR_SEQ 545..672
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_005233"
FT VARIANT 200
FT /note="P -> T (in dbSNP:rs3792268)"
FT /evidence="ECO:0000269|PubMed:11017071"
FT /id="VAR_014437"
FT VARIANT 202
FT /note="R -> H (in dbSNP:rs768407925)"
FT /evidence="ECO:0000269|PubMed:11017071"
FT /id="VAR_014438"
FT VARIANT 276
FT /note="E -> G (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036049"
FT VARIANT 341
FT /note="A -> V (in dbSNP:rs776848131)"
FT /evidence="ECO:0000269|PubMed:11017071"
FT /id="VAR_014439"
FT VARIANT 504
FT /note="T -> A (in dbSNP:rs7607759)"
FT /evidence="ECO:0000269|PubMed:11017071,
FT ECO:0000269|PubMed:14702039"
FT /id="VAR_014440"
FT VARIANT 529
FT /note="A -> S"
FT /evidence="ECO:0000269|PubMed:11017071"
FT /id="VAR_014441"
FT VARIANT 613
FT /note="S -> N (in dbSNP:rs146148004)"
FT /evidence="ECO:0000269|PubMed:11017071"
FT /id="VAR_014442"
FT VARIANT 666
FT /note="I -> V (in dbSNP:rs2975766)"
FT /evidence="ECO:0000269|PubMed:11017071,
FT ECO:0000269|PubMed:11347906, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_014443"
FT CONFLICT 195
FT /note="G -> S (in Ref. 4; BAC11220)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="E -> K (in Ref. 1; AAG17969/AAG17971)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 672 AA; 74952 MW; 74A48D879E896C71 CRC64;
MRAGRGATPA RELFRDAAFP AADSSLFCDL STPLAQFRED ITWRRPQEIC ATPRLFPDDP
REGQVKQGLL GDCWFLCACA ALQKSRHLLD QVIPPGQPSW ADQEYRGSFT CRIWQFGRWV
EVTTDDRLPC LAGRLCFSRC QREDVFWLPL LEKVYAKVHG SYEHLWAGQV ADALVDLTGG
LAERWNLKGV AGSGGQQDRP GRWEHRTCRQ LLHLKDQCLI SCCVLSPRAG ARELGEFHAF
IVSDLRELQG QAGQCILLLR IQNPWGRRCW QGLWREGGEG WSQVDAAVAS ELLSQLQEGE
FWVEEEEFLR EFDELTVGYP VTEAGHLQSL YTERLLCHTR ALPGAWVKGQ SAGGCRNNSG
FPSNPKFWLR VSEPSEVYIA VLQRSRLHAA DWAGRARALV GDSHTSWSPA SIPGKHYQAV
GLHLWKVEKR RVNLPRVLSM PPVAGTACHA YDREVHLRCE LSPGYYLAVP STFLKDAPGE
FLLRVFSTGR VSLSAIRAVA KNTTPGAALP AGEWGTVQLR GSWRVGQTAG GSRNFASYPT
NPCFPFSVPE GPGPRCVRIT LHQHCRPSDT EFHPIGFHIF QVPEGGRSQD APPLLLQEPL
LSCVPHRYAQ EVSRLCLLPA GTYKVVPSTY LPDTEGAFTV TIATRIDRPS IHSQEMLGQF
LQEVSIMAVM KT
