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 27-MAR-2024, entry version 190. 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. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 240. DR IntAct; Q9NZT1; 59. 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 SwissPalm; Q9NZT1; -. DR BioMuta; CALML5; -. DR DMDM; 215273944; -. DR EPD; Q9NZT1; -. DR jPOST; Q9NZT1; -. DR MassIVE; Q9NZT1; -. DR MaxQB; Q9NZT1; -. DR PaxDb; 9606-ENSP00000369689; -. DR PeptideAtlas; Q9NZT1; -. DR PRIDE; Q9NZT1; -. DR ProteomicsDB; 83506; -. DR TopDownProteomics; Q9NZT1; -. DR Antibodypedia; 24103; 223 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 AGR; HGNC:18180; -. 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; 22601at2759; -. 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 1129 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 cell types or tissues. 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 Gene3D; 1.10.238.10; EF-hand; 2. DR InterPro; IPR011992; EF-hand-dom_pair. DR InterPro; IPR018247; EF_Hand_1_Ca_BS. DR InterPro; IPR002048; EF_hand_dom. DR PANTHER; PTHR23050; CALCIUM BINDING PROTEIN; 1. DR PANTHER; PTHR23050:SF224; CALMODULIN-LIKE PROTEIN 5; 1. DR Pfam; PF13499; EF-hand_7; 2. DR SMART; SM00054; EFh; 4. DR SUPFAM; SSF47473; EF-hand; 1. DR PROSITE; PS00018; EF_HAND_1; 4. DR PROSITE; PS50222; EF_HAND_2; 4. DR Genevisible; Q9NZT1; HS. 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 //