Full text data of CALML3
CALML3
[Confidence: low (only semi-automatic identification from reviews)]
Calmodulin-like protein 3 (CaM-like protein; CLP; Calmodulin-related protein NB-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Calmodulin-like protein 3 (CaM-like protein; CLP; Calmodulin-related protein NB-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P27482
ID CALL3_HUMAN Reviewed; 149 AA.
AC P27482; B2R9V6; Q5SQI4;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 118.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION BY
RP 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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 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 be similar to that of authentic calmodulin and may
CC actually compete with calmodulin by binding, with different
CC affinities, to cellular substrates.
CC -!- INTERACTION:
CC Q9HD67:MYO10; NbExp=2; IntAct=EBI-747537, EBI-307061;
CC -!- TISSUE SPECIFICITY: Expressed in normal mammary, prostate,
CC cervical, and epidermal tissues. It is greatly reduced or
CC undetectable in transformed cells.
CC -!- INDUCTION: By TGFB1.
CC -!- MISCELLANEOUS: Binds four calcium ions.
CC -!- SIMILARITY: Belongs to the calmodulin family.
CC -!- SIMILARITY: Contains 4 EF-hand domains.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M58026; AAA36356.1; -; mRNA.
DR EMBL; X13461; CAA31809.1; -; Genomic_DNA.
DR EMBL; AL732437; CAI11029.1; -; Genomic_DNA.
DR EMBL; AK313934; BAG36653.1; -; mRNA.
DR EMBL; CH471072; EAW86443.1; -; Genomic_DNA.
DR EMBL; BC031889; AAH31889.1; -; mRNA.
DR PIR; A38278; MCHUNB.
DR RefSeq; NP_005176.1; NM_005185.2.
DR UniGene; Hs.239600; -.
DR PDB; 1GGZ; X-ray; 1.50 A; A=2-149.
DR PDBsum; 1GGZ; -.
DR ProteinModelPortal; P27482; -.
DR SMR; P27482; 5-148.
DR IntAct; P27482; 7.
DR MINT; MINT-1440064; -.
DR STRING; 9606.ENSP00000315299; -.
DR PhosphoSite; P27482; -.
DR DMDM; 115502; -.
DR PaxDb; P27482; -.
DR PeptideAtlas; P27482; -.
DR PRIDE; P27482; -.
DR DNASU; 810; -.
DR Ensembl; ENST00000315238; ENSP00000315299; ENSG00000178363.
DR GeneID; 810; -.
DR KEGG; hsa:810; -.
DR UCSC; uc001iie.1; human.
DR CTD; 810; -.
DR GeneCards; GC10P005556; -.
DR HGNC; HGNC:1452; CALML3.
DR HPA; CAB010070; -.
DR MIM; 114184; gene.
DR neXtProt; NX_P27482; -.
DR PharmGKB; PA26044; -.
DR eggNOG; COG5126; -.
DR HOGENOM; HOG000233018; -.
DR HOVERGEN; HBG012180; -.
DR InParanoid; P27482; -.
DR KO; K02183; -.
DR OMA; CITTQEL; -.
DR OrthoDB; EOG7F7WBV; -.
DR PhylomeDB; P27482; -.
DR ChiTaRS; CALML3; human.
DR EvolutionaryTrace; P27482; -.
DR GeneWiki; CALML3; -.
DR GenomeRNAi; 810; -.
DR NextBio; 3288; -.
DR PRO; PR:P27482; -.
DR Bgee; P27482; -.
DR CleanEx; HS_CALML3; -.
DR Genevestigator; P27482; -.
DR GO; GO:0005509; F:calcium ion binding; TAS:ProtInc.
DR Gene3D; 1.10.238.10; -; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF00036; EF-hand_1; 3.
DR Pfam; PF13405; EF-hand_6; 1.
DR SMART; SM00054; EFh; 4.
DR PROSITE; PS00018; EF_HAND_1; 4.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Complete proteome; Metal-binding;
KW Reference proteome; Repeat.
FT CHAIN 1 149 Calmodulin-like protein 3.
FT /FTId=PRO_0000073547.
FT DOMAIN 8 43 EF-hand 1.
FT DOMAIN 44 79 EF-hand 2.
FT DOMAIN 81 116 EF-hand 3.
FT DOMAIN 117 149 EF-hand 4.
FT CA_BIND 21 32 1.
FT CA_BIND 57 68 2.
FT CA_BIND 94 105 3.
FT CA_BIND 130 141 4.
FT HELIX 7 20
FT STRAND 25 28
FT HELIX 30 39
FT HELIX 46 54
FT STRAND 61 65
FT HELIX 66 93
FT STRAND 98 101
FT HELIX 103 112
FT HELIX 119 129
FT STRAND 133 138
FT HELIX 139 147
SQ SEQUENCE 149 AA; 16891 MW; 1AB883E8ED4D263D CRC64;
MADQLTEEQV TEFKEAFSLF DKDGDGCITT RELGTVMRSL GQNPTEAELR DMMSEIDRDG
NGTVDFPEFL GMMARKMKDT DNEEEIREAF RVFDKDGNGF VSAAELRHVM TRLGEKLSDE
EVDEMIRAAD TDGDGQVNYE EFVRVLVSK
//
ID CALL3_HUMAN Reviewed; 149 AA.
AC P27482; B2R9V6; Q5SQI4;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 118.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION BY
RP 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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 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 be similar to that of authentic calmodulin and may
CC actually compete with calmodulin by binding, with different
CC affinities, to cellular substrates.
CC -!- INTERACTION:
CC Q9HD67:MYO10; NbExp=2; IntAct=EBI-747537, EBI-307061;
CC -!- TISSUE SPECIFICITY: Expressed in normal mammary, prostate,
CC cervical, and epidermal tissues. It is greatly reduced or
CC undetectable in transformed cells.
CC -!- INDUCTION: By TGFB1.
CC -!- MISCELLANEOUS: Binds four calcium ions.
CC -!- SIMILARITY: Belongs to the calmodulin family.
CC -!- SIMILARITY: Contains 4 EF-hand domains.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M58026; AAA36356.1; -; mRNA.
DR EMBL; X13461; CAA31809.1; -; Genomic_DNA.
DR EMBL; AL732437; CAI11029.1; -; Genomic_DNA.
DR EMBL; AK313934; BAG36653.1; -; mRNA.
DR EMBL; CH471072; EAW86443.1; -; Genomic_DNA.
DR EMBL; BC031889; AAH31889.1; -; mRNA.
DR PIR; A38278; MCHUNB.
DR RefSeq; NP_005176.1; NM_005185.2.
DR UniGene; Hs.239600; -.
DR PDB; 1GGZ; X-ray; 1.50 A; A=2-149.
DR PDBsum; 1GGZ; -.
DR ProteinModelPortal; P27482; -.
DR SMR; P27482; 5-148.
DR IntAct; P27482; 7.
DR MINT; MINT-1440064; -.
DR STRING; 9606.ENSP00000315299; -.
DR PhosphoSite; P27482; -.
DR DMDM; 115502; -.
DR PaxDb; P27482; -.
DR PeptideAtlas; P27482; -.
DR PRIDE; P27482; -.
DR DNASU; 810; -.
DR Ensembl; ENST00000315238; ENSP00000315299; ENSG00000178363.
DR GeneID; 810; -.
DR KEGG; hsa:810; -.
DR UCSC; uc001iie.1; human.
DR CTD; 810; -.
DR GeneCards; GC10P005556; -.
DR HGNC; HGNC:1452; CALML3.
DR HPA; CAB010070; -.
DR MIM; 114184; gene.
DR neXtProt; NX_P27482; -.
DR PharmGKB; PA26044; -.
DR eggNOG; COG5126; -.
DR HOGENOM; HOG000233018; -.
DR HOVERGEN; HBG012180; -.
DR InParanoid; P27482; -.
DR KO; K02183; -.
DR OMA; CITTQEL; -.
DR OrthoDB; EOG7F7WBV; -.
DR PhylomeDB; P27482; -.
DR ChiTaRS; CALML3; human.
DR EvolutionaryTrace; P27482; -.
DR GeneWiki; CALML3; -.
DR GenomeRNAi; 810; -.
DR NextBio; 3288; -.
DR PRO; PR:P27482; -.
DR Bgee; P27482; -.
DR CleanEx; HS_CALML3; -.
DR Genevestigator; P27482; -.
DR GO; GO:0005509; F:calcium ion binding; TAS:ProtInc.
DR Gene3D; 1.10.238.10; -; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF00036; EF-hand_1; 3.
DR Pfam; PF13405; EF-hand_6; 1.
DR SMART; SM00054; EFh; 4.
DR PROSITE; PS00018; EF_HAND_1; 4.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Complete proteome; Metal-binding;
KW Reference proteome; Repeat.
FT CHAIN 1 149 Calmodulin-like protein 3.
FT /FTId=PRO_0000073547.
FT DOMAIN 8 43 EF-hand 1.
FT DOMAIN 44 79 EF-hand 2.
FT DOMAIN 81 116 EF-hand 3.
FT DOMAIN 117 149 EF-hand 4.
FT CA_BIND 21 32 1.
FT CA_BIND 57 68 2.
FT CA_BIND 94 105 3.
FT CA_BIND 130 141 4.
FT HELIX 7 20
FT STRAND 25 28
FT HELIX 30 39
FT HELIX 46 54
FT STRAND 61 65
FT HELIX 66 93
FT STRAND 98 101
FT HELIX 103 112
FT HELIX 119 129
FT STRAND 133 138
FT HELIX 139 147
SQ SEQUENCE 149 AA; 16891 MW; 1AB883E8ED4D263D CRC64;
MADQLTEEQV TEFKEAFSLF DKDGDGCITT RELGTVMRSL GQNPTEAELR DMMSEIDRDG
NGTVDFPEFL GMMARKMKDT DNEEEIREAF RVFDKDGNGF VSAAELRHVM TRLGEKLSDE
EVDEMIRAAD TDGDGQVNYE EFVRVLVSK
//
MIM
114184
*RECORD*
*FIELD* NO
114184
*FIELD* TI
*114184 CALMODULIN-LIKE 3; CALML3
;;CALMODULIN-LIKE PROTEIN; CLP
*FIELD* TX
CLONING
read more
Using calmodulin (CALM1; 114180) as probe, Koller and Strehler, (1988)
cloned CALML3, which they designated GH6, from a leukocyte genomic
library. The deduced 148-amino acid protein contains 4 helix-loop-helix
Ca(2+)-binding motifs and shares 85% identity with vertebrate
calmodulin. Northern blot analysis detected no expression in fibroblast,
teratoma, or erythroleukemia cell lines.
By immunohistochemical staining, Rogers et al. (2001) determined the
tissue distribution of CALML3, which they designated CLP. CLP was
expressed exclusively in the epithelium of the tissues surveyed and was
most abundant in thyroid, breast, prostate, kidney, and skin. CLP
expression appeared to increase in stratified epithelium during
differentiation, as illustrated in skin, where CLP staining intensified
from the basal through the spinous to the granular layers.
BIOCHEMICAL FEATURES
Qian et al. (1998) determined the secondary structure of CLP complexed
with Ca(2+) by multidimensional nuclear magnetic resonance spectroscopy.
Overall, CLP has a 2-domain structure similar to that of calmodulin.
Qian et al. (1998) identified differences between calmodulin and CLP in
the lengths of several helical elements and, most importantly, in the
central nonhelical flexible region. Their analysis suggested that the
sum of small differences in the central regions of calmodulin and CLP
plays a crucial role in target selectivity between these proteins.
Han et al. (2002) determined the 1.5-angstrom crystal structure of CLP
and compared it with that of calmodulin. They verified that CLP contains
2 globular domains connected by a central 7-turn alpha helix. Each
globular domain has 2 helix-loop-helix motifs that form the 4
Ca(2+)-binding sites. The central helix of CLP is less flexible than the
central helix of calmodulin, and the 2 proteins differ in the
orientation of the globular domains about the hinge region. Significant
differences between the electric surface potentials at the target
protein-binding regions of CLP and calmodulin suggested that the ranges
of CLP and calmodulin target proteins do not fully overlap.
GENE FUNCTION
Rogers et al. (2001) examined the expression of CLP in cultured normal
human keratinocytes in response to various agents known to affect
keratinocyte differentiation. They found that agents that inhibit
terminal differentiation, particularly epidermal growth factor (EGF;
131530), downregulate CLP expression. Using several other agents that
affect the growth and differentiation of keratinocytes, Rogers et al.
(2001) determined that upregulated expression of CLP mRNA is linked to
initiation of terminal differentiation.
Using gel overlays and yeast 2-hybrid screens, Rogers and Strehler
(2001) identified myosin X (MYO10; 601481) as a specific
Ca(2+)-dependent binding partner for CLP. CLP specifically bound to
motif 3 of the IQ domain of MYO10, and both proteins colocalized at the
cell periphery of mammary carcinoma cells. Rogers and Strehler (2001)
concluded that CLP is a specific light chain of MYO10 in vivo.
GENE STRUCTURE
Koller and Strehler (1988) determined that the CALML3 gene contains a
single exon. The upstream region has no obvious TATA box, but it does
have a putative CAAT box. The promoter region has several CGAGG and
CACCC repeat sequences and a putative cAMP responsive element.
MAPPING
Berchtold et al. (1993) mapped a functional intronless gene coding for
CLP to chromosome 10pter-p13. Chromosomal assignment was performed by
Southern blot analysis of DNA from human/rodent somatic cell hybrids and
amplification of a gene-specific 1,090-bp DNA fragment by PCR from DNA
of human/hamster cell hybrids. Chromosomal sublocalization was carried
out by in situ hybridization.
*FIELD* RF
1. Berchtold, M. W.; Koller, M.; Egli, R.; Rhyner, J. A.; Hameister,
H.; Strehler, E. E.: Localization of the intronless gene coding for
calmodulin-like protein CLP to human chromosome 10p13-ter. Hum. Genet. 90:
496-500, 1993.
2. Han, B.-G.; Han, M.; Sui, H.; Yaswen, P.; Walian, P. J.; Jap, B.
K.: Crystal structure of human calmodulin-like protein: insights
into its functional role. FEBS Lett. 521: 24-30, 2002.
3. Koller, M.; Strehler, E. E.: Characterization of an intronless
human calmodulin-like pseudogene. FEBS Lett. 239: 121-128, 1988.
4. Qian, H.; Rogers, M. S.; Schleucher, J.; Edlund, U.; Strehler,
E. E.; Sethson, I.: Sequential assignment of (1)H, (15)N, (13)C resonances
and secondary structure of human calmodulin-like protein determined
by NMR spectroscopy. Protein Sci. 7: 2421-2430, 1998.
5. Rogers, M. S.; Kobayashi, T.; Pittelkow, M. R.; Strehler, E. E.
: Human calmodulin-like protein is an epithelial-specific protein
regulated during keratinocyte differentiation. Exp. Cell Res. 267:
216-224, 2001.
6. Rogers, M. S.; Strehler, E. E.: The tumor-sensitive calmodulin-like
protein is a specific light chain of human unconventional myosin X. J.
Biol. Chem. 276: 12182-12189, 2001.
*FIELD* CN
Patricia A. Hartz - updated: 11/12/2002
*FIELD* CD
Victor A. McKusick: 12/23/1993
*FIELD* ED
mgross: 11/12/2002
carol: 12/23/1993
*RECORD*
*FIELD* NO
114184
*FIELD* TI
*114184 CALMODULIN-LIKE 3; CALML3
;;CALMODULIN-LIKE PROTEIN; CLP
*FIELD* TX
CLONING
read more
Using calmodulin (CALM1; 114180) as probe, Koller and Strehler, (1988)
cloned CALML3, which they designated GH6, from a leukocyte genomic
library. The deduced 148-amino acid protein contains 4 helix-loop-helix
Ca(2+)-binding motifs and shares 85% identity with vertebrate
calmodulin. Northern blot analysis detected no expression in fibroblast,
teratoma, or erythroleukemia cell lines.
By immunohistochemical staining, Rogers et al. (2001) determined the
tissue distribution of CALML3, which they designated CLP. CLP was
expressed exclusively in the epithelium of the tissues surveyed and was
most abundant in thyroid, breast, prostate, kidney, and skin. CLP
expression appeared to increase in stratified epithelium during
differentiation, as illustrated in skin, where CLP staining intensified
from the basal through the spinous to the granular layers.
BIOCHEMICAL FEATURES
Qian et al. (1998) determined the secondary structure of CLP complexed
with Ca(2+) by multidimensional nuclear magnetic resonance spectroscopy.
Overall, CLP has a 2-domain structure similar to that of calmodulin.
Qian et al. (1998) identified differences between calmodulin and CLP in
the lengths of several helical elements and, most importantly, in the
central nonhelical flexible region. Their analysis suggested that the
sum of small differences in the central regions of calmodulin and CLP
plays a crucial role in target selectivity between these proteins.
Han et al. (2002) determined the 1.5-angstrom crystal structure of CLP
and compared it with that of calmodulin. They verified that CLP contains
2 globular domains connected by a central 7-turn alpha helix. Each
globular domain has 2 helix-loop-helix motifs that form the 4
Ca(2+)-binding sites. The central helix of CLP is less flexible than the
central helix of calmodulin, and the 2 proteins differ in the
orientation of the globular domains about the hinge region. Significant
differences between the electric surface potentials at the target
protein-binding regions of CLP and calmodulin suggested that the ranges
of CLP and calmodulin target proteins do not fully overlap.
GENE FUNCTION
Rogers et al. (2001) examined the expression of CLP in cultured normal
human keratinocytes in response to various agents known to affect
keratinocyte differentiation. They found that agents that inhibit
terminal differentiation, particularly epidermal growth factor (EGF;
131530), downregulate CLP expression. Using several other agents that
affect the growth and differentiation of keratinocytes, Rogers et al.
(2001) determined that upregulated expression of CLP mRNA is linked to
initiation of terminal differentiation.
Using gel overlays and yeast 2-hybrid screens, Rogers and Strehler
(2001) identified myosin X (MYO10; 601481) as a specific
Ca(2+)-dependent binding partner for CLP. CLP specifically bound to
motif 3 of the IQ domain of MYO10, and both proteins colocalized at the
cell periphery of mammary carcinoma cells. Rogers and Strehler (2001)
concluded that CLP is a specific light chain of MYO10 in vivo.
GENE STRUCTURE
Koller and Strehler (1988) determined that the CALML3 gene contains a
single exon. The upstream region has no obvious TATA box, but it does
have a putative CAAT box. The promoter region has several CGAGG and
CACCC repeat sequences and a putative cAMP responsive element.
MAPPING
Berchtold et al. (1993) mapped a functional intronless gene coding for
CLP to chromosome 10pter-p13. Chromosomal assignment was performed by
Southern blot analysis of DNA from human/rodent somatic cell hybrids and
amplification of a gene-specific 1,090-bp DNA fragment by PCR from DNA
of human/hamster cell hybrids. Chromosomal sublocalization was carried
out by in situ hybridization.
*FIELD* RF
1. Berchtold, M. W.; Koller, M.; Egli, R.; Rhyner, J. A.; Hameister,
H.; Strehler, E. E.: Localization of the intronless gene coding for
calmodulin-like protein CLP to human chromosome 10p13-ter. Hum. Genet. 90:
496-500, 1993.
2. Han, B.-G.; Han, M.; Sui, H.; Yaswen, P.; Walian, P. J.; Jap, B.
K.: Crystal structure of human calmodulin-like protein: insights
into its functional role. FEBS Lett. 521: 24-30, 2002.
3. Koller, M.; Strehler, E. E.: Characterization of an intronless
human calmodulin-like pseudogene. FEBS Lett. 239: 121-128, 1988.
4. Qian, H.; Rogers, M. S.; Schleucher, J.; Edlund, U.; Strehler,
E. E.; Sethson, I.: Sequential assignment of (1)H, (15)N, (13)C resonances
and secondary structure of human calmodulin-like protein determined
by NMR spectroscopy. Protein Sci. 7: 2421-2430, 1998.
5. Rogers, M. S.; Kobayashi, T.; Pittelkow, M. R.; Strehler, E. E.
: Human calmodulin-like protein is an epithelial-specific protein
regulated during keratinocyte differentiation. Exp. Cell Res. 267:
216-224, 2001.
6. Rogers, M. S.; Strehler, E. E.: The tumor-sensitive calmodulin-like
protein is a specific light chain of human unconventional myosin X. J.
Biol. Chem. 276: 12182-12189, 2001.
*FIELD* CN
Patricia A. Hartz - updated: 11/12/2002
*FIELD* CD
Victor A. McKusick: 12/23/1993
*FIELD* ED
mgross: 11/12/2002
carol: 12/23/1993