CALL5_HUMAN
ID CALL5_HUMAN Reviewed; 146 AA.
AC Q9NZT1; Q5SQI3; Q8IXU8;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 181.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 human
RT 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., 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLY-58 AND 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 2-50, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hepatoma;
RA Bienvenut W.V., Dhillon A.S., Kolch W.;
RL Submitted (FEB-2008) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [6]
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 CLSP.";
RL Structure 14:1029-1038(2006).
RN [7]
RP VARIANTS GLY-58 AND ARG-74, AND IDENTIFICATION BY 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 orthogonal
RT analysis of shotgun proteomics data.";
RL J. Proteome Res. 6:2331-2340(2007).
CC -!- FUNCTION: Binds calcium. May be involved in terminal differentiation of
CC keratinocytes.
CC -!- SUBUNIT: Associates with transglutaminase 3.
CC -!- TISSUE SPECIFICITY: Particularly abundant in the epidermis where its
CC expression is directly related to keratinocyte differentiation. Very
CC low expression in lung.
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DR EMBL; AF172852; AAF66821.1; -; mRNA.
DR EMBL; AL732437; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC039172; AAH39172.1; -; mRNA.
DR CCDS; CCDS7068.1; -.
DR RefSeq; NP_059118.2; NM_017422.4.
DR PDB; 2B1U; NMR; -; A=76-146.
DR PDBsum; 2B1U; -.
DR AlphaFoldDB; Q9NZT1; -.
DR SMR; Q9NZT1; -.
DR BioGRID; 119732; 226.
DR IntAct; Q9NZT1; 54.
DR MINT; Q9NZT1; -.
DR STRING; 9606.ENSP00000369689; -.
DR GlyGen; Q9NZT1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NZT1; -.
DR PhosphoSitePlus; Q9NZT1; -.
DR BioMuta; CALML5; -.
DR DMDM; 215273944; -.
DR EPD; Q9NZT1; -.
DR jPOST; Q9NZT1; -.
DR MassIVE; Q9NZT1; -.
DR MaxQB; Q9NZT1; -.
DR PaxDb; Q9NZT1; -.
DR PeptideAtlas; Q9NZT1; -.
DR PRIDE; Q9NZT1; -.
DR ProteomicsDB; 83506; -.
DR TopDownProteomics; Q9NZT1; -.
DR Antibodypedia; 24103; 205 antibodies from 26 providers.
DR DNASU; 51806; -.
DR Ensembl; ENST00000380332.5; ENSP00000369689.3; ENSG00000178372.8.
DR GeneID; 51806; -.
DR KEGG; hsa:51806; -.
DR MANE-Select; ENST00000380332.5; ENSP00000369689.3; NM_017422.5; NP_059118.2.
DR UCSC; uc001iic.3; human.
DR CTD; 51806; -.
DR DisGeNET; 51806; -.
DR GeneCards; CALML5; -.
DR HGNC; HGNC:18180; CALML5.
DR HPA; ENSG00000178372; Tissue enriched (skin).
DR MIM; 605183; gene.
DR neXtProt; NX_Q9NZT1; -.
DR OpenTargets; ENSG00000178372; -.
DR PharmGKB; PA134862009; -.
DR VEuPathDB; HostDB:ENSG00000178372; -.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00940000163406; -.
DR HOGENOM; CLU_061288_2_0_1; -.
DR InParanoid; Q9NZT1; -.
DR OMA; VKRMKSW; -.
DR OrthoDB; 1386217at2759; -.
DR PhylomeDB; Q9NZT1; -.
DR TreeFam; TF300912; -.
DR PathwayCommons; Q9NZT1; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q9NZT1; -.
DR BioGRID-ORCS; 51806; 10 hits in 1057 CRISPR screens.
DR EvolutionaryTrace; Q9NZT1; -.
DR GeneWiki; CALML5; -.
DR GenomeRNAi; 51806; -.
DR Pharos; Q9NZT1; Tbio.
DR PRO; PR:Q9NZT1; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9NZT1; protein.
DR Bgee; ENSG00000178372; Expressed in skin of abdomen and 86 other tissues.
DR Genevisible; Q9NZT1; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
DR GO; GO:0008544; P:epidermis development; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
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; Acetylation; Calcium; Direct protein sequencing;
KW Metal-binding; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.4"
FT CHAIN 2..146
FT /note="Calmodulin-like protein 5"
FT /id="PRO_0000073854"
FT DOMAIN 8..43
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 44..74
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 78..113
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 114..146
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 91
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 93
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 95
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 97
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 102
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 127
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 129
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 131
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 133
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 138
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.4"
FT VARIANT 58
FT /note="S -> G (confirmed at protein level;
FT dbSNP:rs11546426)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17488105"
FT /id="VAR_047545"
FT VARIANT 74
FT /note="K -> R (confirmed at protein level;
FT dbSNP:rs10904516)"
FT /evidence="ECO:0000269|PubMed:10777582,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17488105"
FT /id="VAR_047546"
FT HELIX 80..87
FT /evidence="ECO:0007829|PDB:2B1U"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:2B1U"
FT HELIX 100..106
FT /evidence="ECO:0007829|PDB:2B1U"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:2B1U"
FT HELIX 116..125
FT /evidence="ECO:0007829|PDB:2B1U"
FT STRAND 128..135
FT /evidence="ECO:0007829|PDB:2B1U"
FT HELIX 138..143
FT /evidence="ECO:0007829|PDB:2B1U"
SQ SEQUENCE 146 AA; 15893 MW; 70746291268494CC CRC64;
MAGELTPEEE AQYKKAFSAV DTDGNGTINA QELGAALKAT GKNLSEAQLR KLISEVDSDG
DGEISFQEFL TAAKKARAGL EDLQVAFRAF DQDGDGHITV DELRRAMAGL GQPLPQEELD
AMIREADVDQ DGRVNYEEFA RMLAQE
