CALL3_HUMAN
ID CALL3_HUMAN Reviewed; 149 AA.
AC P27482; B2R9V6; Q5SQI4;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Calmodulin-like protein 3;
DE AltName: Full=CaM-like protein;
DE Short=CLP;
DE AltName: Full=Calmodulin-related protein NB-1;
GN Name=CALML3;
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], TISSUE SPECIFICITY, AND INDUCTION BY TGFB1.
RX PubMed=2217169; DOI=10.1073/pnas.87.19.7360;
RA Yaswen P., Smoll A., Peehl D.M., Trask D.K., Sager R., Stampfer M.R.;
RT "Down-regulation of a calmodulin-related gene during transformation of
RT human mammary epithelial cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:7360-7364(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3181418; DOI=10.1016/0014-5793(88)80558-1;
RA Koller M., Strehler E.E.;
RT "Characterization of an intronless human calmodulin-like pseudogene.";
RL FEBS Lett. 239:121-128(1988).
RN [3]
RP SEQUENCE REVISION.
RA Koller M.;
RL Submitted (JAN-1992) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Esophagus;
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=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [8]
RP CHARACTERIZATION.
RX PubMed=1334432; DOI=10.1021/bi00166a017;
RA Rhyner J.A., Koller M., Durussel-Gerber I., Cox J.A., Strehler E.E.;
RT "Characterization of the human calmodulin-like protein expressed in
RT Escherichia coli.";
RL Biochemistry 31:12826-12832(1992).
RN [9]
RP FUNCTION, AND INTERACTION WITH MYO10.
RX PubMed=11278607; DOI=10.1074/jbc.m010056200;
RA Rogers M.S., Strehler E.E.;
RT "The tumor-sensitive calmodulin-like protein is a specific light chain of
RT human unconventional myosin X.";
RL J. Biol. Chem. 276:12182-12189(2001).
RN [10]
RP FUNCTION.
RX PubMed=18295593; DOI=10.1016/j.bbrc.2008.02.056;
RA Bennett R.D., Strehler E.E.;
RT "Calmodulin-like protein enhances myosin-10 translation.";
RL Biochem. Biophys. Res. Commun. 369:654-659(2008).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
RX PubMed=12067719; DOI=10.1016/s0014-5793(02)02780-1;
RA Han B.G., Han M., Sui H., Yaswen P., Walian P.J., Jap B.K.;
RT "Crystal structure of human calmodulin-like protein: insights into its
RT functional role.";
RL FEBS Lett. 521:24-30(2002).
CC -!- FUNCTION: May function as a specific light chain of unconventional
CC myosin-10 (MYO10), also enhances MYO10 translation, possibly by acting
CC as a chaperone for the emerging MYO10 heavy chain protein. May compete
CC with calmodulin by binding, with different affinities, to cellular
CC substrates. {ECO:0000269|PubMed:11278607, ECO:0000269|PubMed:18295593}.
CC -!- SUBUNIT: Interacts with MYO10, the interaction is calcium-dependent and
CC essential for MYO10 function in filopodial extension.
CC {ECO:0000269|PubMed:11278607}.
CC -!- INTERACTION:
CC P27482; Q15051-2: IQCB1; NbExp=3; IntAct=EBI-747537, EBI-11944935;
CC P27482; Q9H0B3: IQCN; NbExp=4; IntAct=EBI-747537, EBI-745878;
CC P27482; A0JP07: KIAA1683; NbExp=3; IntAct=EBI-747537, EBI-10171456;
CC P27482; Q8NCR3: MFI; NbExp=3; IntAct=EBI-747537, EBI-744790;
CC P27482; Q9HD67: MYO10; NbExp=3; IntAct=EBI-747537, EBI-307061;
CC P27482; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-747537, EBI-750109;
CC -!- TISSUE SPECIFICITY: Expressed in normal mammary, prostate, cervical,
CC and epidermal tissues. It is greatly reduced or undetectable in
CC transformed cells. {ECO:0000269|PubMed:2217169}.
CC -!- INDUCTION: By TGFB1. {ECO:0000269|PubMed:2217169}.
CC -!- MISCELLANEOUS: Binds four calcium ions.
CC -!- SIMILARITY: Belongs to the calmodulin family. {ECO:0000305}.
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DR EMBL; M58026; AAA36356.1; -; mRNA.
DR EMBL; X13461; CAA31809.1; -; Genomic_DNA.
DR EMBL; AL732437; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK313934; BAG36653.1; -; mRNA.
DR EMBL; CH471072; EAW86443.1; -; Genomic_DNA.
DR EMBL; BC031889; AAH31889.1; -; mRNA.
DR CCDS; CCDS7069.1; -.
DR PIR; A38278; MCHUNB.
DR RefSeq; NP_005176.1; NM_005185.3.
DR PDB; 1GGZ; X-ray; 1.50 A; A=2-149.
DR PDBsum; 1GGZ; -.
DR AlphaFoldDB; P27482; -.
DR SMR; P27482; -.
DR BioGRID; 107261; 265.
DR IntAct; P27482; 66.
DR MINT; P27482; -.
DR STRING; 9606.ENSP00000315299; -.
DR iPTMnet; P27482; -.
DR PhosphoSitePlus; P27482; -.
DR BioMuta; CALML3; -.
DR DMDM; 115502; -.
DR EPD; P27482; -.
DR jPOST; P27482; -.
DR MassIVE; P27482; -.
DR MaxQB; P27482; -.
DR PaxDb; P27482; -.
DR PeptideAtlas; P27482; -.
DR PRIDE; P27482; -.
DR ProteomicsDB; 54395; -.
DR TopDownProteomics; P27482; -.
DR Antibodypedia; 24109; 138 antibodies from 22 providers.
DR DNASU; 810; -.
DR Ensembl; ENST00000315238.3; ENSP00000315299.1; ENSG00000178363.5.
DR GeneID; 810; -.
DR KEGG; hsa:810; -.
DR MANE-Select; ENST00000315238.3; ENSP00000315299.1; NM_005185.4; NP_005176.1.
DR UCSC; uc001iie.2; human.
DR CTD; 810; -.
DR DisGeNET; 810; -.
DR GeneCards; CALML3; -.
DR HGNC; HGNC:1452; CALML3.
DR HPA; ENSG00000178363; Tissue enhanced (esophagus, skin, vagina).
DR MIM; 114184; gene.
DR neXtProt; NX_P27482; -.
DR OpenTargets; ENSG00000178363; -.
DR PharmGKB; PA26044; -.
DR VEuPathDB; HostDB:ENSG00000178363; -.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00950000182980; -.
DR HOGENOM; CLU_061288_2_0_1; -.
DR InParanoid; P27482; -.
DR OMA; NMIGEID; -.
DR OrthoDB; 1386217at2759; -.
DR PhylomeDB; P27482; -.
DR TreeFam; TF300912; -.
DR PathwayCommons; P27482; -.
DR SignaLink; P27482; -.
DR BioGRID-ORCS; 810; 14 hits in 1066 CRISPR screens.
DR ChiTaRS; CALML3; human.
DR EvolutionaryTrace; P27482; -.
DR GeneWiki; CALML3; -.
DR GenomeRNAi; 810; -.
DR Pharos; P27482; Tbio.
DR PRO; PR:P27482; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P27482; protein.
DR Bgee; ENSG00000178363; Expressed in lower esophagus mucosa and 113 other tissues.
DR Genevisible; P27482; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
DR CDD; cd00051; EFh; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13499; EF-hand_7; 2.
DR SMART; SM00054; EFh; 4.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 4.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Metal-binding; Reference proteome; Repeat.
FT CHAIN 1..149
FT /note="Calmodulin-like protein 3"
FT /id="PRO_0000073547"
FT DOMAIN 8..43
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 44..79
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 81..116
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 117..149
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 21
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 23
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 25
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 61
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 94
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 96
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 98
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 105
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 130
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 134
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 136
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 141
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT HELIX 7..20
FT /evidence="ECO:0007829|PDB:1GGZ"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:1GGZ"
FT HELIX 30..39
FT /evidence="ECO:0007829|PDB:1GGZ"
FT HELIX 46..54
FT /evidence="ECO:0007829|PDB:1GGZ"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:1GGZ"
FT HELIX 66..93
FT /evidence="ECO:0007829|PDB:1GGZ"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:1GGZ"
FT HELIX 103..112
FT /evidence="ECO:0007829|PDB:1GGZ"
FT HELIX 119..129
FT /evidence="ECO:0007829|PDB:1GGZ"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:1GGZ"
FT HELIX 139..147
FT /evidence="ECO:0007829|PDB:1GGZ"
SQ SEQUENCE 149 AA; 16891 MW; 1AB883E8ED4D263D CRC64;
MADQLTEEQV TEFKEAFSLF DKDGDGCITT RELGTVMRSL GQNPTEAELR DMMSEIDRDG
NGTVDFPEFL GMMARKMKDT DNEEEIREAF RVFDKDGNGF VSAAELRHVM TRLGEKLSDE
EVDEMIRAAD TDGDGQVNYE EFVRVLVSK
