Full text data of CALML5
CALML5
(CLSP)
[Confidence: low (only semi-automatic identification from reviews)]
Calmodulin-like protein 5 (Calmodulin-like skin protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Calmodulin-like protein 5 (Calmodulin-like skin protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9NZT1
ID CALL5_HUMAN Reviewed; 146 AA.
AC Q9NZT1; Q5SQI3; Q8IXU8;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 25-NOV-2008, sequence version 2.
DT 22-JAN-2014, entry version 116.
DE RecName: Full=Calmodulin-like protein 5;
DE AltName: Full=Calmodulin-like skin protein;
GN Name=CALML5; Synonyms=CLSP;
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], CHARACTERIZATION, AND VARIANT ARG-74.
RC TISSUE=Skin;
RX PubMed=10777582; DOI=10.1074/jbc.275.17.12841;
RA Mehul B., Bernard D., Simonetti L., Bernard M.A., Schmidt R.;
RT "Identification and cloning of a new calmodulin-like protein from
RT human epidermis.";
RL J. Biol. Chem. 275:12841-12847(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLY-58 AND
RP ARG-74.
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 [4]
RP PROTEIN SEQUENCE OF 2-50, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Hepatoma;
RA Bienvenut W.V., Dhillon A.S., Kolch W.;
RL Submitted (FEB-2008) to UniProtKB.
RN [5]
RP STRUCTURE BY NMR OF 76-146, AND CALCIUM-BINDING.
RX PubMed=16765896; DOI=10.1016/j.str.2006.04.004;
RA Babini E., Bertini I., Capozzi F., Chirivino E., Luchinat C.;
RT "A structural and dynamic characterization of the EF-hand protein
RT CLSP.";
RL Structure 14:1029-1038(2006).
RN [6]
RP VARIANTS GLY-58 AND ARG-74, AND MASS SPECTROMETRY.
RX PubMed=17488105; DOI=10.1021/pr0700908;
RA Bunger M.K., Cargile B.J., Sevinsky J.R., Deyanova E., Yates N.A.,
RA Hendrickson R.C., Stephenson J.L. Jr.;
RT "Detection and validation of non-synonymous coding SNPs from
RT orthogonal analysis of shotgun proteomics data.";
RL J. Proteome Res. 6:2331-2340(2007).
CC -!- FUNCTION: Binds calcium. May be involved in terminal
CC differentiation of keratinocytes.
CC -!- SUBUNIT: Associates with transglutaminase 3.
CC -!- TISSUE SPECIFICITY: Particularly abundant in the epidermis where
CC its expression is directly related to keratinocyte
CC differentiation. Very low expression in lung.
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; AF172852; AAF66821.1; -; mRNA.
DR EMBL; AL732437; CAI11030.1; -; Genomic_DNA.
DR EMBL; BC039172; AAH39172.1; -; mRNA.
DR RefSeq; NP_059118.2; NM_017422.4.
DR UniGene; Hs.180142; -.
DR PDB; 2B1U; NMR; -; A=76-146.
DR PDBsum; 2B1U; -.
DR ProteinModelPortal; Q9NZT1; -.
DR SMR; Q9NZT1; 2-146.
DR IntAct; Q9NZT1; 4.
DR MINT; MINT-5003638; -.
DR STRING; 9606.ENSP00000369689; -.
DR PhosphoSite; Q9NZT1; -.
DR DMDM; 215273944; -.
DR PaxDb; Q9NZT1; -.
DR PRIDE; Q9NZT1; -.
DR DNASU; 51806; -.
DR Ensembl; ENST00000380332; ENSP00000369689; ENSG00000178372.
DR GeneID; 51806; -.
DR KEGG; hsa:51806; -.
DR UCSC; uc001iic.2; human.
DR CTD; 51806; -.
DR GeneCards; GC10M005530; -.
DR H-InvDB; HIX0025916; -.
DR HGNC; HGNC:18180; CALML5.
DR HPA; HPA040725; -.
DR MIM; 605183; gene.
DR neXtProt; NX_Q9NZT1; -.
DR PharmGKB; PA134862009; -.
DR eggNOG; COG5126; -.
DR HOGENOM; HOG000233018; -.
DR HOVERGEN; HBG012180; -.
DR InParanoid; Q9NZT1; -.
DR KO; K02183; -.
DR OMA; NYEEFAR; -.
DR OrthoDB; EOG7GBFZP; -.
DR PhylomeDB; Q9NZT1; -.
DR EvolutionaryTrace; Q9NZT1; -.
DR GeneWiki; CALML5; -.
DR GenomeRNAi; 51806; -.
DR NextBio; 55928; -.
DR PRO; PR:Q9NZT1; -.
DR Bgee; Q9NZT1; -.
DR CleanEx; HS_CALML5; -.
DR Genevestigator; Q9NZT1; -.
DR GO; GO:0005509; F:calcium ion binding; TAS:ProtInc.
DR GO; GO:0008544; P:epidermis development; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 1.10.238.10; -; 1.
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 PROSITE; PS00018; EF_HAND_1; 4.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Calcium; Complete proteome;
KW Direct protein sequencing; Metal-binding; Polymorphism;
KW Reference proteome; Repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 146 Calmodulin-like protein 5.
FT /FTId=PRO_0000073854.
FT DOMAIN 8 43 EF-hand 1.
FT DOMAIN 44 77 EF-hand 2.
FT DOMAIN 78 113 EF-hand 3.
FT DOMAIN 114 146 EF-hand 4.
FT CA_BIND 21 32 1.
FT CA_BIND 57 68 2 (Potential).
FT CA_BIND 91 102 3 (Potential).
FT CA_BIND 127 138 4 (Potential).
FT MOD_RES 2 2 N-acetylalanine.
FT VARIANT 58 58 S -> G (polymorphism confirmed at protein
FT level; dbSNP:rs11546426).
FT /FTId=VAR_047545.
FT VARIANT 74 74 K -> R (polymorphism confirmed at protein
FT level; dbSNP:rs10904516).
FT /FTId=VAR_047546.
FT HELIX 80 87
FT STRAND 93 99
FT HELIX 100 106
FT HELIX 107 109
FT HELIX 116 125
FT STRAND 128 135
FT HELIX 138 143
SQ SEQUENCE 146 AA; 15893 MW; 70746291268494CC CRC64;
MAGELTPEEE AQYKKAFSAV DTDGNGTINA QELGAALKAT GKNLSEAQLR KLISEVDSDG
DGEISFQEFL TAAKKARAGL EDLQVAFRAF DQDGDGHITV DELRRAMAGL GQPLPQEELD
AMIREADVDQ DGRVNYEEFA RMLAQE
//
ID CALL5_HUMAN Reviewed; 146 AA.
AC Q9NZT1; Q5SQI3; Q8IXU8;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 25-NOV-2008, sequence version 2.
DT 22-JAN-2014, entry version 116.
DE RecName: Full=Calmodulin-like protein 5;
DE AltName: Full=Calmodulin-like skin protein;
GN Name=CALML5; Synonyms=CLSP;
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], CHARACTERIZATION, AND VARIANT ARG-74.
RC TISSUE=Skin;
RX PubMed=10777582; DOI=10.1074/jbc.275.17.12841;
RA Mehul B., Bernard D., Simonetti L., Bernard M.A., Schmidt R.;
RT "Identification and cloning of a new calmodulin-like protein from
RT human epidermis.";
RL J. Biol. Chem. 275:12841-12847(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLY-58 AND
RP ARG-74.
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 [4]
RP PROTEIN SEQUENCE OF 2-50, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Hepatoma;
RA Bienvenut W.V., Dhillon A.S., Kolch W.;
RL Submitted (FEB-2008) to UniProtKB.
RN [5]
RP STRUCTURE BY NMR OF 76-146, AND CALCIUM-BINDING.
RX PubMed=16765896; DOI=10.1016/j.str.2006.04.004;
RA Babini E., Bertini I., Capozzi F., Chirivino E., Luchinat C.;
RT "A structural and dynamic characterization of the EF-hand protein
RT CLSP.";
RL Structure 14:1029-1038(2006).
RN [6]
RP VARIANTS GLY-58 AND ARG-74, AND MASS SPECTROMETRY.
RX PubMed=17488105; DOI=10.1021/pr0700908;
RA Bunger M.K., Cargile B.J., Sevinsky J.R., Deyanova E., Yates N.A.,
RA Hendrickson R.C., Stephenson J.L. Jr.;
RT "Detection and validation of non-synonymous coding SNPs from
RT orthogonal analysis of shotgun proteomics data.";
RL J. Proteome Res. 6:2331-2340(2007).
CC -!- FUNCTION: Binds calcium. May be involved in terminal
CC differentiation of keratinocytes.
CC -!- SUBUNIT: Associates with transglutaminase 3.
CC -!- TISSUE SPECIFICITY: Particularly abundant in the epidermis where
CC its expression is directly related to keratinocyte
CC differentiation. Very low expression in lung.
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; AF172852; AAF66821.1; -; mRNA.
DR EMBL; AL732437; CAI11030.1; -; Genomic_DNA.
DR EMBL; BC039172; AAH39172.1; -; mRNA.
DR RefSeq; NP_059118.2; NM_017422.4.
DR UniGene; Hs.180142; -.
DR PDB; 2B1U; NMR; -; A=76-146.
DR PDBsum; 2B1U; -.
DR ProteinModelPortal; Q9NZT1; -.
DR SMR; Q9NZT1; 2-146.
DR IntAct; Q9NZT1; 4.
DR MINT; MINT-5003638; -.
DR STRING; 9606.ENSP00000369689; -.
DR PhosphoSite; Q9NZT1; -.
DR DMDM; 215273944; -.
DR PaxDb; Q9NZT1; -.
DR PRIDE; Q9NZT1; -.
DR DNASU; 51806; -.
DR Ensembl; ENST00000380332; ENSP00000369689; ENSG00000178372.
DR GeneID; 51806; -.
DR KEGG; hsa:51806; -.
DR UCSC; uc001iic.2; human.
DR CTD; 51806; -.
DR GeneCards; GC10M005530; -.
DR H-InvDB; HIX0025916; -.
DR HGNC; HGNC:18180; CALML5.
DR HPA; HPA040725; -.
DR MIM; 605183; gene.
DR neXtProt; NX_Q9NZT1; -.
DR PharmGKB; PA134862009; -.
DR eggNOG; COG5126; -.
DR HOGENOM; HOG000233018; -.
DR HOVERGEN; HBG012180; -.
DR InParanoid; Q9NZT1; -.
DR KO; K02183; -.
DR OMA; NYEEFAR; -.
DR OrthoDB; EOG7GBFZP; -.
DR PhylomeDB; Q9NZT1; -.
DR EvolutionaryTrace; Q9NZT1; -.
DR GeneWiki; CALML5; -.
DR GenomeRNAi; 51806; -.
DR NextBio; 55928; -.
DR PRO; PR:Q9NZT1; -.
DR Bgee; Q9NZT1; -.
DR CleanEx; HS_CALML5; -.
DR Genevestigator; Q9NZT1; -.
DR GO; GO:0005509; F:calcium ion binding; TAS:ProtInc.
DR GO; GO:0008544; P:epidermis development; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 1.10.238.10; -; 1.
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 PROSITE; PS00018; EF_HAND_1; 4.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Calcium; Complete proteome;
KW Direct protein sequencing; Metal-binding; Polymorphism;
KW Reference proteome; Repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 146 Calmodulin-like protein 5.
FT /FTId=PRO_0000073854.
FT DOMAIN 8 43 EF-hand 1.
FT DOMAIN 44 77 EF-hand 2.
FT DOMAIN 78 113 EF-hand 3.
FT DOMAIN 114 146 EF-hand 4.
FT CA_BIND 21 32 1.
FT CA_BIND 57 68 2 (Potential).
FT CA_BIND 91 102 3 (Potential).
FT CA_BIND 127 138 4 (Potential).
FT MOD_RES 2 2 N-acetylalanine.
FT VARIANT 58 58 S -> G (polymorphism confirmed at protein
FT level; dbSNP:rs11546426).
FT /FTId=VAR_047545.
FT VARIANT 74 74 K -> R (polymorphism confirmed at protein
FT level; dbSNP:rs10904516).
FT /FTId=VAR_047546.
FT HELIX 80 87
FT STRAND 93 99
FT HELIX 100 106
FT HELIX 107 109
FT HELIX 116 125
FT STRAND 128 135
FT HELIX 138 143
SQ SEQUENCE 146 AA; 15893 MW; 70746291268494CC CRC64;
MAGELTPEEE AQYKKAFSAV DTDGNGTINA QELGAALKAT GKNLSEAQLR KLISEVDSDG
DGEISFQEFL TAAKKARAGL EDLQVAFRAF DQDGDGHITV DELRRAMAGL GQPLPQEELD
AMIREADVDQ DGRVNYEEFA RMLAQE
//
MIM
605183
*RECORD*
*FIELD* NO
605183
*FIELD* TI
*605183 CALMODULIN-LIKE 5; CALML5
;;CALMODULIN-LIKE SKIN PROTEIN; CLSP
*FIELD* TX
read moreCLONING
The stratum corneum, the uppermost layer of the human epidermis,
provides the vital barrier between the organism and its environment. It
is generated by keratinocytes that migrate from the basal layer to the
surface of the epidermis undergoing terminal differentiation, a process
that is calcium dependent. Low concentrations of calcium in the basal
layer of the epidermis favor keratinocyte proliferation, and an
increasing calcium gradient toward the surface controls part of the
complex differentiation. Thus, calcium-binding proteins, which mediate
calcium signals by interacting with and modulating specific target
proteins, are important for epidermal differentiation. Using
2-dimensional gel electrophoresis, Mehul et al. (2000) separated an
extract of total proteins from human stratum corneum. Peptide sequence
analysis of 2 spots, followed by a homology search, revealed
identification of a novel calcium-binding protein of the calmodulin
(e.g., CALM1; 114180) family that the authors named 'calmodulin-like
skin protein' (CLSP). By PCR using a degenerate oligonucleotide based on
a CLSP peptide sequence, and 2 human keratinocyte cDNA libraries, one
derived from proliferating cultured keratinocytes and the other from
differentiated keratinocytes of reconstructed epidermis, Mehul et al.
(2000) isolated a full-length CLSP cDNA. The predicted 146-amino acid
CLSP protein contains 4 putative EF-hands, which are domains that bind
to calcium, 2 potential sites for N-glycosylation, multiple potential
sites for phosphorylation, and 1 potential site for myristoylation. CLSP
shares 52% amino acid sequence homology with human calmodulin. RT-PCR of
various human tissues and reconstructed epidermis detected abundant CLSP
expression only in epidermis, with very low expression in lung.
Evaluation of CLSP expression during keratinocyte differentiation
revealed that CLSP was not detectably expressed in proliferating
keratinocytes but was expressed in differentiating keratinocytes,
beginning at an advanced stage of differentiation.
Hwang and Morasso (2003) cloned mouse Scarf (skin calmodulin-related
factor), the likely ortholog of human CLSP. The deduced 148-amino acid
Scarf protein contains 4 EF-hand domains and shares 64.9% identity with
human CLSP. Scarf has a slightly extended central helix compared with
human CLSP. Northern and RNA dot blot analyses of adult mouse tissues
detected Scarf only in thyroid and skeletal muscle. Northern blot
analysis and RT-PCR showed strong Scarf expression in keratinocytes,
with expression first detected at embryonic day 15. In situ
hybridization localized Scarf within the spinous and granular layers in
stratified epidermis, but not in the basal layer, of 16-day mouse
embryos. In situ hybridization and immunohistochemical analysis of
neonatal skin revealed Scarf only in anucleated differentiated layers of
stratified epidermis. Hwang and Morasso (2003) noted that both Scarf and
human CLSP are expressed predominantly in differentiated keratinocytes,
but that Scarf is expressed earlier than CLSP during the differentiation
process. In addition, Scarf and CLSP show slightly different
distributions in other tissues.
GENE FUNCTION
Mehul et al. (2000) demonstrated that recombinant CLSP could bind
calcium, and like calmodulin, thereafter exposed hydrophobic regions,
which most likely interact with target proteins. Sequencing of an
epidermal protein retained by a CLSP affinity column revealed 100%
identity with transglutaminase-3 (TGM3; 600238), which is a key enzyme
in terminal epidermal differentiation. Mehul et al. (2000) suggested
that CLSP may play an important role in late keratinocyte
differentiation.
Hwang and Morasso (2003) showed that mouse Scarf could bind Ca(2+) in an
in vitro Ca(2+)-binding assay. Mutations in each of the EF-hand motifs
diminished the ability of Scarf to bind Ca(2+).
MAPPING
Hartz (2010) mapped the CALML5 gene to chromosome 10p15.1, based on an
alignment of the CALML5 sequence (GenBank GENBANK AF172852) with the
genomic sequence (GRCh37).
Hwang and Morasso (2003) found that the mouse Scarf gene is duplicated.
The 2 copies, Scarf and Scarf2, map about 15 kb apart on chromosome 13.
This region of mouse chromosome 13 appears syntenic with human
chromosome 10, but humans do not have an ortholog of Scarf2.
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 11/22/2010.
2. Hwang, M.; Morasso, M. I.: The novel murine Ca(2+)-binding protein,
Scarf, is differentially expressed during epidermal differentiation. J.
Biol. Chem. 278: 47827-47833, 2003.
3. Mehul, B.; Bernard, D.; Simonetti, L.; Bernard, M. A.; Schmidt,
R.: Identification and cloning of a new calmodulin-like protein from
human epidermis. J. Biol. Chem. 275: 12841-12847, 2000.
*FIELD* CN
Patricia A. Hartz - updated: 11/22/2010
*FIELD* CD
Patti M. Sherman: 7/31/2000
*FIELD* ED
mgross: 11/23/2010
terry: 11/22/2010
terry: 5/10/2006
alopez: 1/3/2006
mcapotos: 8/4/2000
psherman: 8/1/2000
*RECORD*
*FIELD* NO
605183
*FIELD* TI
*605183 CALMODULIN-LIKE 5; CALML5
;;CALMODULIN-LIKE SKIN PROTEIN; CLSP
*FIELD* TX
read moreCLONING
The stratum corneum, the uppermost layer of the human epidermis,
provides the vital barrier between the organism and its environment. It
is generated by keratinocytes that migrate from the basal layer to the
surface of the epidermis undergoing terminal differentiation, a process
that is calcium dependent. Low concentrations of calcium in the basal
layer of the epidermis favor keratinocyte proliferation, and an
increasing calcium gradient toward the surface controls part of the
complex differentiation. Thus, calcium-binding proteins, which mediate
calcium signals by interacting with and modulating specific target
proteins, are important for epidermal differentiation. Using
2-dimensional gel electrophoresis, Mehul et al. (2000) separated an
extract of total proteins from human stratum corneum. Peptide sequence
analysis of 2 spots, followed by a homology search, revealed
identification of a novel calcium-binding protein of the calmodulin
(e.g., CALM1; 114180) family that the authors named 'calmodulin-like
skin protein' (CLSP). By PCR using a degenerate oligonucleotide based on
a CLSP peptide sequence, and 2 human keratinocyte cDNA libraries, one
derived from proliferating cultured keratinocytes and the other from
differentiated keratinocytes of reconstructed epidermis, Mehul et al.
(2000) isolated a full-length CLSP cDNA. The predicted 146-amino acid
CLSP protein contains 4 putative EF-hands, which are domains that bind
to calcium, 2 potential sites for N-glycosylation, multiple potential
sites for phosphorylation, and 1 potential site for myristoylation. CLSP
shares 52% amino acid sequence homology with human calmodulin. RT-PCR of
various human tissues and reconstructed epidermis detected abundant CLSP
expression only in epidermis, with very low expression in lung.
Evaluation of CLSP expression during keratinocyte differentiation
revealed that CLSP was not detectably expressed in proliferating
keratinocytes but was expressed in differentiating keratinocytes,
beginning at an advanced stage of differentiation.
Hwang and Morasso (2003) cloned mouse Scarf (skin calmodulin-related
factor), the likely ortholog of human CLSP. The deduced 148-amino acid
Scarf protein contains 4 EF-hand domains and shares 64.9% identity with
human CLSP. Scarf has a slightly extended central helix compared with
human CLSP. Northern and RNA dot blot analyses of adult mouse tissues
detected Scarf only in thyroid and skeletal muscle. Northern blot
analysis and RT-PCR showed strong Scarf expression in keratinocytes,
with expression first detected at embryonic day 15. In situ
hybridization localized Scarf within the spinous and granular layers in
stratified epidermis, but not in the basal layer, of 16-day mouse
embryos. In situ hybridization and immunohistochemical analysis of
neonatal skin revealed Scarf only in anucleated differentiated layers of
stratified epidermis. Hwang and Morasso (2003) noted that both Scarf and
human CLSP are expressed predominantly in differentiated keratinocytes,
but that Scarf is expressed earlier than CLSP during the differentiation
process. In addition, Scarf and CLSP show slightly different
distributions in other tissues.
GENE FUNCTION
Mehul et al. (2000) demonstrated that recombinant CLSP could bind
calcium, and like calmodulin, thereafter exposed hydrophobic regions,
which most likely interact with target proteins. Sequencing of an
epidermal protein retained by a CLSP affinity column revealed 100%
identity with transglutaminase-3 (TGM3; 600238), which is a key enzyme
in terminal epidermal differentiation. Mehul et al. (2000) suggested
that CLSP may play an important role in late keratinocyte
differentiation.
Hwang and Morasso (2003) showed that mouse Scarf could bind Ca(2+) in an
in vitro Ca(2+)-binding assay. Mutations in each of the EF-hand motifs
diminished the ability of Scarf to bind Ca(2+).
MAPPING
Hartz (2010) mapped the CALML5 gene to chromosome 10p15.1, based on an
alignment of the CALML5 sequence (GenBank GENBANK AF172852) with the
genomic sequence (GRCh37).
Hwang and Morasso (2003) found that the mouse Scarf gene is duplicated.
The 2 copies, Scarf and Scarf2, map about 15 kb apart on chromosome 13.
This region of mouse chromosome 13 appears syntenic with human
chromosome 10, but humans do not have an ortholog of Scarf2.
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 11/22/2010.
2. Hwang, M.; Morasso, M. I.: The novel murine Ca(2+)-binding protein,
Scarf, is differentially expressed during epidermal differentiation. J.
Biol. Chem. 278: 47827-47833, 2003.
3. Mehul, B.; Bernard, D.; Simonetti, L.; Bernard, M. A.; Schmidt,
R.: Identification and cloning of a new calmodulin-like protein from
human epidermis. J. Biol. Chem. 275: 12841-12847, 2000.
*FIELD* CN
Patricia A. Hartz - updated: 11/22/2010
*FIELD* CD
Patti M. Sherman: 7/31/2000
*FIELD* ED
mgross: 11/23/2010
terry: 11/22/2010
terry: 5/10/2006
alopez: 1/3/2006
mcapotos: 8/4/2000
psherman: 8/1/2000