CALB1_HUMAN
ID CALB1_HUMAN Reviewed; 261 AA.
AC P05937; B2R696; B7Z9J4;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Calbindin;
DE AltName: Full=Calbindin D28;
DE AltName: Full=D-28K;
DE AltName: Full=Vitamin D-dependent calcium-binding protein, avian-type;
GN Name=CALB1; Synonyms=CAB27;
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] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=3691519; DOI=10.1111/j.1432-1033.1987.tb13688.x;
RA Parmentier M., Lawson D.E.M., Vassart G.;
RT "Human 27-kDa calbindin complementary DNA sequence. Evolutionary and
RT functional implications.";
RL Eur. J. Biochem. 170:207-215(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Amygdala, Cerebellum, and Substantia nigra;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney, and Lung;
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42 AND 201-261.
RC TISSUE=Brain;
RX PubMed=2565876; DOI=10.1016/0888-7543(89)90335-2;
RA Parmentier M., de Vijlder J.J.M., Muir E., Szpirer C., Islam M.Q.,
RA Geurts van Kessel A., Lawson D.E.M., Vassart G.;
RT "The human calbindin 27-kDa gene: structural organization of the 5' and 3'
RT regions, chromosomal assignment, and restriction fragment length
RT polymorphism.";
RL Genomics 4:309-319(1989).
RN [7]
RP INTERACTION WITH RANBP9.
RX PubMed=12684061; DOI=10.1016/s0006-291x(03)00499-6;
RA Lutz W., Frank E.M., Craig T.A., Thompson R., Venters R.A., Kojetin D.,
RA Cavanagh J., Kumar R.;
RT "Calbindin D28K interacts with Ran-binding protein M: identification of
RT interacting domains by NMR spectroscopy.";
RL Biochem. Biophys. Res. Commun. 303:1186-1192(2003).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9] {ECO:0007744|PDB:6FIE}
RP X-RAY CRYSTALLOGRAPHY (1.51 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS, AND
RP DOMAIN.
RX PubMed=30289411; DOI=10.1107/s2059798318011610;
RA Noble J.W., Almalki R., Roe S.M., Wagner A., Duman R., Atack J.R.;
RT "The X-ray structure of human calbindin-D28K: an improved model.";
RL Acta Crystallogr. D 74:1008-1014(2018).
CC -!- FUNCTION: Buffers cytosolic calcium. May stimulate a membrane Ca(2+)-
CC ATPase and a 3',5'-cyclic nucleotide phosphodiesterase.
CC -!- SUBUNIT: Interacts with RANBP9. {ECO:0000269|PubMed:12684061}.
CC -!- INTERACTION:
CC P05937; Q96IK1-2: BOD1; NbExp=3; IntAct=EBI-4286943, EBI-18924329;
CC P05937; Q9Y6K9: IKBKG; NbExp=3; IntAct=EBI-4286943, EBI-81279;
CC P05937; Q9NQA5: TRPV5; NbExp=4; IntAct=EBI-4286943, EBI-751281;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P05937-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P05937-2; Sequence=VSP_055508;
CC -!- DOMAIN: This protein has four functional calcium-binding sites;
CC potential sites II and VI have lost affinity for calcium.
CC {ECO:0000269|PubMed:30289411}.
CC -!- SIMILARITY: Belongs to the calbindin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Calbindin entry;
CC URL="https://en.wikipedia.org/wiki/Calbindin";
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DR EMBL; X06661; CAA29860.1; -; mRNA.
DR EMBL; AF068862; AAC62230.1; -; Genomic_DNA.
DR EMBL; AC004612; AAC14672.1; -; Genomic_DNA.
DR EMBL; AK054881; BAG51438.1; -; mRNA.
DR EMBL; AK312491; BAG35393.1; -; mRNA.
DR EMBL; AK315959; BAH14330.1; -; mRNA.
DR EMBL; AF049895; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC123779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471060; EAW91665.1; -; Genomic_DNA.
DR EMBL; CH471060; EAW91666.1; -; Genomic_DNA.
DR EMBL; BC006478; AAH06478.1; -; mRNA.
DR EMBL; BC020864; AAH20864.1; -; mRNA.
DR EMBL; M19878; AAA98991.1; -; Genomic_DNA.
DR EMBL; M19879; AAA98992.1; -; Genomic_DNA.
DR CCDS; CCDS6251.1; -. [P05937-1]
DR PIR; S00234; S00234.
DR RefSeq; NP_004920.1; NM_004929.3. [P05937-1]
DR PDB; 6FIE; X-ray; 1.51 A; B=1-261.
DR PDBsum; 6FIE; -.
DR AlphaFoldDB; P05937; -.
DR SASBDB; P05937; -.
DR SMR; P05937; -.
DR BioGRID; 107244; 6.
DR IntAct; P05937; 6.
DR MINT; P05937; -.
DR STRING; 9606.ENSP00000265431; -.
DR DrugBank; DB11093; Calcium citrate.
DR DrugBank; DB11348; Calcium Phosphate.
DR DrugBank; DB14481; Calcium phosphate dihydrate.
DR GlyConnect; 1056; 3 N-Linked glycans (1 site).
DR GlyGen; P05937; 1 site, 3 N-linked glycans (1 site).
DR iPTMnet; P05937; -.
DR PhosphoSitePlus; P05937; -.
DR BioMuta; CALB1; -.
DR EPD; P05937; -.
DR jPOST; P05937; -.
DR MassIVE; P05937; -.
DR MaxQB; P05937; -.
DR PaxDb; P05937; -.
DR PeptideAtlas; P05937; -.
DR PRIDE; P05937; -.
DR ProteomicsDB; 51862; -. [P05937-1]
DR ProteomicsDB; 7034; -.
DR ABCD; P05937; 2 sequenced antibodies.
DR Antibodypedia; 3678; 482 antibodies from 45 providers.
DR DNASU; 793; -.
DR Ensembl; ENST00000265431.7; ENSP00000265431.3; ENSG00000104327.7. [P05937-1]
DR Ensembl; ENST00000518457.5; ENSP00000429602.1; ENSG00000104327.7. [P05937-2]
DR GeneID; 793; -.
DR KEGG; hsa:793; -.
DR MANE-Select; ENST00000265431.7; ENSP00000265431.3; NM_004929.4; NP_004920.1.
DR UCSC; uc003yel.2; human. [P05937-1]
DR CTD; 793; -.
DR DisGeNET; 793; -.
DR GeneCards; CALB1; -.
DR HGNC; HGNC:1434; CALB1.
DR HPA; ENSG00000104327; Tissue enriched (kidney).
DR MIM; 114050; gene.
DR neXtProt; NX_P05937; -.
DR OpenTargets; ENSG00000104327; -.
DR PharmGKB; PA26026; -.
DR VEuPathDB; HostDB:ENSG00000104327; -.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00950000183108; -.
DR HOGENOM; CLU_054826_1_1_1; -.
DR InParanoid; P05937; -.
DR OMA; EEFMQTW; -.
DR OrthoDB; 979297at2759; -.
DR PhylomeDB; P05937; -.
DR TreeFam; TF325083; -.
DR BRENDA; 3.1.3.25; 2681.
DR PathwayCommons; P05937; -.
DR Reactome; R-HSA-977225; Amyloid fiber formation.
DR SignaLink; P05937; -.
DR BioGRID-ORCS; 793; 9 hits in 1082 CRISPR screens.
DR ChiTaRS; CALB1; human.
DR GenomeRNAi; 793; -.
DR Pharos; P05937; Tbio.
DR PRO; PR:P05937; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P05937; protein.
DR Bgee; ENSG00000104327; Expressed in nephron tubule and 135 other tissues.
DR ExpressionAtlas; P05937; baseline and differential.
DR Genevisible; P05937; HS.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0044305; C:calyx of Held; IEA:Ensembl.
DR GO; GO:0032437; C:cuticular plate; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IEA:Ensembl.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0099524; C:postsynaptic cytosol; IEA:Ensembl.
DR GO; GO:0099523; C:presynaptic cytosol; IEA:Ensembl.
DR GO; GO:0032420; C:stereocilium; IEA:Ensembl.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0043195; C:terminal bouton; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0099567; F:calcium ion binding involved in regulation of postsynaptic cytosolic calcium ion concentration; IEA:Ensembl.
DR GO; GO:0099534; F:calcium ion binding involved in regulation of presynaptic cytosolic calcium ion concentration; IEA:Ensembl.
DR GO; GO:0005499; F:vitamin D binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IMP:UniProtKB.
DR GO; GO:0071310; P:cellular response to organic substance; IEA:Ensembl.
DR GO; GO:0090102; P:cochlea development; IEA:Ensembl.
DR GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR GO; GO:0007616; P:long-term memory; IMP:UniProtKB.
DR GO; GO:0072205; P:metanephric collecting duct development; IEA:Ensembl.
DR GO; GO:0072286; P:metanephric connecting tubule development; IEA:Ensembl.
DR GO; GO:0072221; P:metanephric distal convoluted tubule development; IEA:Ensembl.
DR GO; GO:0035502; P:metanephric part of ureteric bud development; IEA:Ensembl.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:1900271; P:regulation of long-term synaptic potentiation; IBA:GO_Central.
DR GO; GO:0099509; P:regulation of presynaptic cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0010842; P:retina layer formation; IEA:Ensembl.
DR GO; GO:0007614; P:short-term memory; IMP:UniProtKB.
DR InterPro; IPR029634; Calbindin.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR PANTHER; PTHR19972:SF14; PTHR19972:SF14; 1.
DR Pfam; PF00036; EF-hand_1; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 4.
DR SUPFAM; SSF47473; SSF47473; 2.
DR PROSITE; PS00018; EF_HAND_1; 4.
DR PROSITE; PS50222; EF_HAND_2; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Calcium; Metal-binding;
KW Reference proteome; Repeat; Vitamin D.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P04467"
FT CHAIN 2..261
FT /note="Calbindin"
FT /id="PRO_0000073472"
FT DOMAIN 11..46
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 53..88
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 98..133
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 142..177
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 186..221
FT /note="EF-hand 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 2..7
FT /note="Interaction with RANBP9"
FT /evidence="ECO:0000269|PubMed:12684061"
FT BINDING 24
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:30289411, ECO:0007744|PDB:6FIE"
FT BINDING 26
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:30289411, ECO:0007744|PDB:6FIE"
FT BINDING 28
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:30289411, ECO:0007744|PDB:6FIE"
FT BINDING 30
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:30289411, ECO:0007744|PDB:6FIE"
FT BINDING 35
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:30289411, ECO:0007744|PDB:6FIE"
FT BINDING 111
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:30289411, ECO:0007744|PDB:6FIE"
FT BINDING 113
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:30289411, ECO:0007744|PDB:6FIE"
FT BINDING 115
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:30289411, ECO:0007744|PDB:6FIE"
FT BINDING 122
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:30289411, ECO:0007744|PDB:6FIE"
FT BINDING 155
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:30289411, ECO:0007744|PDB:6FIE"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:30289411, ECO:0007744|PDB:6FIE"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:30289411, ECO:0007744|PDB:6FIE"
FT BINDING 161
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:30289411, ECO:0007744|PDB:6FIE"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:30289411, ECO:0007744|PDB:6FIE"
FT BINDING 199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:30289411, ECO:0007744|PDB:6FIE"
FT BINDING 201
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:30289411, ECO:0007744|PDB:6FIE"
FT BINDING 203
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:30289411, ECO:0007744|PDB:6FIE"
FT BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:30289411, ECO:0007744|PDB:6FIE"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:30289411, ECO:0007744|PDB:6FIE"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P04467"
FT VAR_SEQ 1..57
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055508"
FT HELIX 2..5
FT /evidence="ECO:0007829|PDB:6FIE"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:6FIE"
FT HELIX 13..23
FT /evidence="ECO:0007829|PDB:6FIE"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:6FIE"
FT HELIX 34..49
FT /evidence="ECO:0007829|PDB:6FIE"
FT HELIX 56..62
FT /evidence="ECO:0007829|PDB:6FIE"
FT HELIX 75..81
FT /evidence="ECO:0007829|PDB:6FIE"
FT HELIX 86..90
FT /evidence="ECO:0007829|PDB:6FIE"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:6FIE"
FT HELIX 100..110
FT /evidence="ECO:0007829|PDB:6FIE"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:6FIE"
FT HELIX 120..133
FT /evidence="ECO:0007829|PDB:6FIE"
FT HELIX 140..154
FT /evidence="ECO:0007829|PDB:6FIE"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:6FIE"
FT HELIX 164..168
FT /evidence="ECO:0007829|PDB:6FIE"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:6FIE"
FT HELIX 177..184
FT /evidence="ECO:0007829|PDB:6FIE"
FT HELIX 188..198
FT /evidence="ECO:0007829|PDB:6FIE"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:6FIE"
FT HELIX 208..221
FT /evidence="ECO:0007829|PDB:6FIE"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:6FIE"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:6FIE"
FT HELIX 231..239
FT /evidence="ECO:0007829|PDB:6FIE"
FT HELIX 249..256
FT /evidence="ECO:0007829|PDB:6FIE"
SQ SEQUENCE 261 AA; 30025 MW; 8ED7A09BCC5FE5E4 CRC64;
MAESHLQSSL ITASQFFEIW LHFDADGSGY LEGKELQNLI QELQQARKKA GLELSPEMKT
FVDQYGQRDD GKIGIVELAH VLPTEENFLL LFRCQQLKSC EEFMKTWRKY DTDHSGFIET
EELKNFLKDL LEKANKTVDD TKLAEYTDLM LKLFDSNNDG KLELTEMARL LPVQENFLLK
FQGIKMCGKE FNKAFELYDQ DGNGYIDENE LDALLKDLCE KNKQDLDINN ITTYKKNIMA
LSDGGKLYRT DLALILCAGD N
