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Calmodulin-like protein 5 (Calmodulin-like skin protein)

 CALL5_HUMAN             Reviewed;         146 AA.
Q9NZT1; Q5SQI3; Q8IXU8;
01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
25-NOV-2008, sequence version 2.
20-JUN-2018, entry version 156.
RecName: Full=Calmodulin-like protein 5;
AltName: Full=Calmodulin-like skin protein;
Name=CALML5; Synonyms=CLSP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND VARIANT ARG-74.
TISSUE=Skin;
PubMed=10777582; DOI=10.1074/jbc.275.17.12841;
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLY-58 AND
ARG-74.
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 2-50, CLEAVAGE OF INITIATOR METHIONINE,
ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Hepatoma;
Bienvenut W.V., Dhillon A.S., Kolch W.;
Submitted (FEB-2008) to UniProtKB.
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[6]
STRUCTURE BY NMR OF 76-146, AND CALCIUM-BINDING.
PubMed=16765896; DOI=10.1016/j.str.2006.04.004;
Babini E., Bertini I., Capozzi F., Chirivino E., Luchinat C.;
"A structural and dynamic characterization of the EF-hand protein
CLSP.";
Structure 14:1029-1038(2006).
[7]
VARIANTS GLY-58 AND ARG-74, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17488105; DOI=10.1021/pr0700908;
Bunger M.K., Cargile B.J., Sevinsky J.R., Deyanova E., Yates N.A.,
Hendrickson R.C., Stephenson J.L. Jr.;
"Detection and validation of non-synonymous coding SNPs from
orthogonal analysis of shotgun proteomics data.";
J. Proteome Res. 6:2331-2340(2007).
-!- FUNCTION: Binds calcium. May be involved in terminal
differentiation of keratinocytes.
-!- SUBUNIT: Associates with transglutaminase 3.
-!- TISSUE SPECIFICITY: Particularly abundant in the epidermis where
its expression is directly related to keratinocyte
differentiation. Very low expression in lung.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF172852; AAF66821.1; -; mRNA.
EMBL; AL732437; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC039172; AAH39172.1; -; mRNA.
CCDS; CCDS7068.1; -.
RefSeq; NP_059118.2; NM_017422.4.
UniGene; Hs.180142; -.
PDB; 2B1U; NMR; -; A=76-146.
PDBsum; 2B1U; -.
ProteinModelPortal; Q9NZT1; -.
SMR; Q9NZT1; -.
BioGrid; 119732; 46.
IntAct; Q9NZT1; 10.
STRING; 9606.ENSP00000369689; -.
iPTMnet; Q9NZT1; -.
PhosphoSitePlus; Q9NZT1; -.
BioMuta; CALML5; -.
DMDM; 215273944; -.
EPD; Q9NZT1; -.
MaxQB; Q9NZT1; -.
PaxDb; Q9NZT1; -.
PeptideAtlas; Q9NZT1; -.
PRIDE; Q9NZT1; -.
ProteomicsDB; 83506; -.
TopDownProteomics; Q9NZT1; -.
DNASU; 51806; -.
Ensembl; ENST00000380332; ENSP00000369689; ENSG00000178372.
GeneID; 51806; -.
KEGG; hsa:51806; -.
UCSC; uc001iic.3; human.
CTD; 51806; -.
DisGeNET; 51806; -.
EuPathDB; HostDB:ENSG00000178372.7; -.
GeneCards; CALML5; -.
H-InvDB; HIX0025916; -.
HGNC; HGNC:18180; CALML5.
HPA; HPA040725; -.
MIM; 605183; gene.
neXtProt; NX_Q9NZT1; -.
OpenTargets; ENSG00000178372; -.
PharmGKB; PA134862009; -.
eggNOG; KOG0027; Eukaryota.
eggNOG; COG5126; LUCA.
GeneTree; ENSGT00760000118901; -.
HOGENOM; HOG000233018; -.
HOVERGEN; HBG012180; -.
InParanoid; Q9NZT1; -.
KO; K02183; -.
OMA; YKSAFSA; -.
OrthoDB; EOG091G0RVC; -.
PhylomeDB; Q9NZT1; -.
TreeFam; TF300912; -.
Reactome; R-HSA-6798695; Neutrophil degranulation.
EvolutionaryTrace; Q9NZT1; -.
GeneWiki; CALML5; -.
GenomeRNAi; 51806; -.
PRO; PR:Q9NZT1; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000178372; -.
CleanEx; HS_CALML5; -.
Genevisible; Q9NZT1; HS.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0005509; F:calcium ion binding; TAS:ProtInc.
GO; GO:0008544; P:epidermis development; TAS:ProtInc.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
Pfam; PF13499; EF-hand_7; 2.
SMART; SM00054; EFh; 4.
SUPFAM; SSF47473; SSF47473; 1.
PROSITE; PS00018; EF_HAND_1; 4.
PROSITE; PS50222; EF_HAND_2; 4.
1: Evidence at protein level;
3D-structure; Acetylation; Calcium; Complete proteome;
Direct protein sequencing; Metal-binding; Polymorphism;
Reference proteome; Repeat.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.4}.
CHAIN 2 146 Calmodulin-like protein 5.
/FTId=PRO_0000073854.
DOMAIN 8 43 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 44 77 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 78 113 EF-hand 3. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 114 146 EF-hand 4. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 21 32 1.
CA_BIND 57 68 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 91 102 3. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 127 138 4. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
MOD_RES 2 2 N-acetylalanine. {ECO:0000269|Ref.4}.
VARIANT 58 58 S -> G (polymorphism; confirmed at
protein level; dbSNP:rs11546426).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17488105}.
/FTId=VAR_047545.
VARIANT 74 74 K -> R (polymorphism; confirmed at
protein level; dbSNP:rs10904516).
{ECO:0000269|PubMed:10777582,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17488105}.
/FTId=VAR_047546.
HELIX 80 87 {ECO:0000244|PDB:2B1U}.
STRAND 93 99 {ECO:0000244|PDB:2B1U}.
HELIX 100 106 {ECO:0000244|PDB:2B1U}.
HELIX 107 109 {ECO:0000244|PDB:2B1U}.
HELIX 116 125 {ECO:0000244|PDB:2B1U}.
STRAND 128 135 {ECO:0000244|PDB:2B1U}.
HELIX 138 143 {ECO:0000244|PDB:2B1U}.
SEQUENCE 146 AA; 15893 MW; 70746291268494CC CRC64;
MAGELTPEEE AQYKKAFSAV DTDGNGTINA QELGAALKAT GKNLSEAQLR KLISEVDSDG
DGEISFQEFL TAAKKARAGL EDLQVAFRAF DQDGDGHITV DELRRAMAGL GQPLPQEELD
AMIREADVDQ DGRVNYEEFA RMLAQE


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