ID CALB2_HUMAN Reviewed; 271 AA. AC P22676; A8K4Y1; Q53HD2; Q96BK4; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 27-JUN-2006, sequence version 2. DT 27-MAR-2024, entry version 187. DE RecName: Full=Calretinin; DE Short=CR; DE AltName: Full=29 kDa calbindin; GN Name=CALB2; Synonyms=CAB29; 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]. RX PubMed=2618861; DOI=10.1007/978-1-4684-5679-0_25; RA Parmentier M.; RT "The human calbindins: cDNA and gene cloning."; RL Adv. Exp. Med. Biol. 255:233-240(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RX PubMed=2001709; DOI=10.1111/j.1432-1033.1991.tb15788.x; RA Parmentier M., Lefort A.; RT "Structure of the human brain calcium-binding protein calretinin and its RT expression in bacteria."; RL Eur. J. Biochem. 196:79-85(1991). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Adipose tissue, and Cerebellum; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Colon; 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). CC -!- FUNCTION: Calretinin is a calcium-binding protein which is abundant in CC auditory neurons. CC -!- TISSUE SPECIFICITY: Brain. 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"; 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; X56667; CAA39991.1; -; mRNA. DR EMBL; X56668; CAA39992.1; -; Genomic_DNA. DR EMBL; AK291096; BAF83785.1; -; mRNA. DR EMBL; AK222495; BAD96215.1; -; mRNA. DR EMBL; AK222648; BAD96368.1; -; mRNA. DR EMBL; BC015484; AAH15484.1; -; mRNA. DR CCDS; CCDS10899.1; -. DR PIR; S14109; A60253. DR RefSeq; NP_001731.2; NM_001740.4. DR RefSeq; NP_009019.1; NM_007088.3. DR AlphaFoldDB; P22676; -. DR SMR; P22676; -. DR BioGRID; 107245; 10. DR IntAct; P22676; 4. DR STRING; 9606.ENSP00000307508; -. DR DrugBank; DB11093; Calcium citrate. DR DrugBank; DB13800; Calcium levulinate. DR DrugBank; DB11348; Calcium Phosphate. DR DrugBank; DB14481; Calcium phosphate dihydrate. DR TCDB; 8.A.82.1.2; the calmodulin calcium binding protein (calmodulin) family. DR iPTMnet; P22676; -. DR PhosphoSitePlus; P22676; -. DR BioMuta; CALB2; -. DR DMDM; 109940061; -. DR REPRODUCTION-2DPAGE; IPI00027264; -. DR EPD; P22676; -. DR jPOST; P22676; -. DR MassIVE; P22676; -. DR MaxQB; P22676; -. DR PaxDb; 9606-ENSP00000307508; -. DR PeptideAtlas; P22676; -. DR ProteomicsDB; 54015; -. DR Pumba; P22676; -. DR ABCD; P22676; 2 sequenced antibodies. DR Antibodypedia; 1545; 830 antibodies from 48 providers. DR DNASU; 794; -. DR Ensembl; ENST00000302628.9; ENSP00000307508.4; ENSG00000172137.19. DR Ensembl; ENST00000635371.2; ENSP00000488916.1; ENSG00000282830.2. DR GeneID; 794; -. DR KEGG; hsa:794; -. DR MANE-Select; ENST00000302628.9; ENSP00000307508.4; NM_001740.5; NP_001731.2. DR UCSC; uc002faa.6; human. DR AGR; HGNC:1435; -. DR CTD; 794; -. DR DisGeNET; 794; -. DR GeneCards; CALB2; -. DR HGNC; HGNC:1435; CALB2. DR HPA; ENSG00000172137; Tissue enhanced (adipose tissue, brain). DR MIM; 114051; gene. DR neXtProt; NX_P22676; -. DR OpenTargets; ENSG00000172137; -. DR PharmGKB; PA26027; -. DR VEuPathDB; HostDB:ENSG00000172137; -. DR eggNOG; KOG0027; Eukaryota. DR GeneTree; ENSGT00950000183108; -. DR InParanoid; P22676; -. DR OMA; IVLCNEP; -. DR OrthoDB; 3218718at2759; -. DR PhylomeDB; P22676; -. DR TreeFam; TF325083; -. DR PathwayCommons; P22676; -. DR SignaLink; P22676; -. DR BioGRID-ORCS; 794; 9 hits in 1137 CRISPR screens. DR GeneWiki; Calretinin; -. DR GenomeRNAi; 794; -. DR Pharos; P22676; Tbio. DR PRO; PR:P22676; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; P22676; Protein. DR Bgee; ENSG00000172137; Expressed in hypothalamus and 94 other cell types or tissues. DR ExpressionAtlas; P22676; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0030425; C:dendrite; IBA:GO_Central. DR GO; GO:0005921; C:gap junction; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; 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; IBA:GO_Central. DR GO; GO:0099534; F:calcium ion binding involved in regulation of presynaptic cytosolic calcium ion concentration; IEA:Ensembl. 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 CDD; cd16177; EFh_HEF_CR; 1. DR Gene3D; 1.10.238.10; EF-hand; 3. DR InterPro; IPR029646; CALB2. DR InterPro; IPR011992; EF-hand-dom_pair. DR InterPro; IPR018247; EF_Hand_1_Ca_BS. DR InterPro; IPR002048; EF_hand_dom. DR PANTHER; PTHR19972; CALBINDIN; 1. DR PANTHER; PTHR19972:SF4; CALRETININ; 1. DR Pfam; PF13405; EF-hand_6; 1. DR Pfam; PF13499; EF-hand_7; 2. DR SMART; SM00054; EFh; 5. DR SUPFAM; SSF47473; EF-hand; 2. DR PROSITE; PS00018; EF_HAND_1; 5. DR PROSITE; PS50222; EF_HAND_2; 5. DR Genevisible; P22676; HS. PE 2: Evidence at transcript level; KW Calcium; Metal-binding; Phosphoprotein; Reference proteome; Repeat. FT CHAIN 1..271 FT /note="Calretinin" FT /id="PRO_0000073479" FT DOMAIN 16..51 FT /note="EF-hand 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 63..98 FT /note="EF-hand 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 107..142 FT /note="EF-hand 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 151..186 FT /note="EF-hand 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 195..230 FT /note="EF-hand 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 235..270 FT /note="EF-hand 6" FT /evidence="ECO:0000305" FT BINDING 29 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 31 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 33 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" 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 BINDING 40 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 76 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 78 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 80 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 82 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 87 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 120 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 122 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 124 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 126 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 131 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 164 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 166 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 168 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 170 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 175 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 208 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 210 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 212 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 214 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 219 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT MOD_RES 214 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P47728" FT CONFLICT 110 FT /note="A -> T (in Ref. 5; AAH15484)" FT /evidence="ECO:0000305" FT CONFLICT 235 FT /note="M -> I (in Ref. 2; CAA39991)" FT /evidence="ECO:0000305" SQ SEQUENCE 271 AA; 31540 MW; 98116AD706079DB9 CRC64; MAGPQQQPPY LHLAELTASQ FLEIWKHFDA DGNGYIEGKE LENFFQELEK ARKGSGMMSK SDNFGEKMKE FMQKYDKNSD GKIEMAELAQ ILPTEENFLL CFRQHVGSSA EFMEAWRKYD TDRSGYIEAN ELKGFLSDLL KKANRPYDEP KLQEYTQTIL RMFDLNGDGK LGLSEMSRLL PVQENFLLKF QGMKLTSEEF NAIFTFYDKD RSGYIDEHEL DALLKDLYEK NKKEMNIQQL TNYRKSVMSL AEAGKLYRKD LEIVLCSEPP M //