ID RCN3_BOVIN Reviewed; 328 AA. AC Q2KJ39; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 1. DT 27-MAR-2024, entry version 101. DE RecName: Full=Reticulocalbin-3 {ECO:0000305}; DE Flags: Precursor; GN Name=RCN3; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Uterus; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Probable molecular chaperone assisting protein biosynthesis CC and transport in the endoplasmic reticulum (By similarity). Required CC for the proper biosynthesis and transport of pulmonary surfactant- CC associated protein A/SP-A, pulmonary surfactant-associated protein CC D/SP-D and the lipid transporter ABCA3 (By similarity). By regulating CC both the proper expression and the degradation through the endoplasmic CC reticulum-associated protein degradation pathway of these proteins CC plays a crucial role in pulmonary surfactant homeostasis (By CC similarity). Has an anti-fibrotic activity by negatively regulating the CC secretion of type I and type III collagens (By similarity). This CC calcium-binding protein also transiently associates with immature PCSK6 CC and regulates its secretion (By similarity). CC {ECO:0000250|UniProtKB:Q8BH97, ECO:0000250|UniProtKB:Q96D15}. CC -!- SUBUNIT: Interacts with PCSK6 (immature form including the propeptide); CC probably involved in the maturation and the secretion of PCSK6. CC {ECO:0000250|UniProtKB:Q96D15}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen CC {ECO:0000250|UniProtKB:Q96D15}. CC -!- PTM: Degraded by PCSK6 and other endoproteases including FURIN and CC PCSK5. {ECO:0000250|UniProtKB:Q96D15}. CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:I6L9G5}. CC -!- SIMILARITY: Belongs to the CREC family. {ECO:0000305}. 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; BC105535; AAI05536.1; -; mRNA. DR RefSeq; NP_001039725.1; NM_001046260.1. DR AlphaFoldDB; Q2KJ39; -. DR STRING; 9913.ENSBTAP00000031823; -. DR GlyCosmos; Q2KJ39; 2 sites, No reported glycans. DR PaxDb; 9913-ENSBTAP00000031823; -. DR Ensembl; ENSBTAT00000031877.3; ENSBTAP00000031823.2; ENSBTAG00000021799.4. DR GeneID; 522073; -. DR KEGG; bta:522073; -. DR CTD; 57333; -. DR VEuPathDB; HostDB:ENSBTAG00000021799; -. DR VGNC; VGNC:33833; RCN3. DR eggNOG; KOG4223; Eukaryota. DR GeneTree; ENSGT01010000222360; -. DR HOGENOM; CLU_044718_0_1_1; -. DR InParanoid; Q2KJ39; -. DR OMA; QDGKIGW; -. DR TreeFam; TF314849; -. DR Proteomes; UP000009136; Chromosome 18. DR Bgee; ENSBTAG00000021799; Expressed in uterine cervix and 108 other cell types or tissues. DR ExpressionAtlas; Q2KJ39; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell. DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB. DR GO; GO:0032964; P:collagen biosynthetic process; ISS:UniProtKB. DR GO; GO:0036503; P:ERAD pathway; ISS:UniProtKB. DR GO; GO:0060428; P:lung epithelium development; ISS:UniProtKB. DR GO; GO:0055091; P:phospholipid homeostasis; ISS:UniProtKB. DR GO; GO:0010952; P:positive regulation of peptidase activity; ISS:UniProtKB. DR GO; GO:0009306; P:protein secretion; ISS:UniProtKB. DR GO; GO:0015031; P:protein transport; ISS:UniProtKB. DR GO; GO:0043129; P:surfactant homeostasis; ISS:UniProtKB. DR CDD; cd16230; EFh_CREC_RCN3; 1. 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; PTHR10827; RETICULOCALBIN; 1. DR PANTHER; PTHR10827:SF47; RETICULOCALBIN-3; 1. DR Pfam; PF13202; EF-hand_5; 1. DR Pfam; PF13499; EF-hand_7; 1. DR SMART; SM00054; EFh; 3. DR SUPFAM; SSF47473; EF-hand; 2. DR PROSITE; PS00018; EF_HAND_1; 4. DR PROSITE; PS50222; EF_HAND_2; 5. DR PROSITE; PS00014; ER_TARGET; 1. PE 2: Evidence at transcript level; KW Calcium; Chaperone; Endoplasmic reticulum; Glycoprotein; Metal-binding; KW Reference proteome; Repeat; Signal. FT SIGNAL 1..20 FT /evidence="ECO:0000255" FT CHAIN 21..328 FT /note="Reticulocalbin-3" FT /id="PRO_0000240340" FT DOMAIN 75..112 FT /note="EF-hand 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 113..148 FT /note="EF-hand 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 163..198 FT /note="EF-hand 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 200..235 FT /note="EF-hand 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 241..276 FT /note="EF-hand 5" FT /evidence="ECO:0000305" FT DOMAIN 277..312 FT /note="EF-hand 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT MOTIF 325..328 FT /note="Prevents secretion from ER" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138" FT BINDING 92 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000305" FT BINDING 94 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000305" FT BINDING 96 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000305" FT BINDING 101 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000305" FT BINDING 126 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 128 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 130 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 132 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 137 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 176 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000305" FT BINDING 178 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000305" FT BINDING 180 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000305" FT BINDING 182 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000305" FT BINDING 187 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000305" FT BINDING 213 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 215 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 217 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 219 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 224 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 254 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000305" FT BINDING 256 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000305" FT BINDING 258 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000305" FT BINDING 260 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000305" FT BINDING 265 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000305" FT BINDING 290 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 292 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 294 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 296 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 301 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT CARBOHYD 140 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 262 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" SQ SEQUENCE 328 AA; 37568 MW; 4D5FB9AF2D81FAEA CRC64; MMWPPSLLLL LLLLRRGAQG KPSPDAGPHG QGRVHHAAPL SEAPHDDAHG NFQYDHEAFL GREVAKEFDQ LTPEESQARL GRIVDRMDRA GDGDGWVSLA ELRSWIAHTQ QRHIRDSVSA AWNTYDTDRD GRVGWEELRN ATYGHYEPGE EFHDVEDAET YKKMLARDER RFRVADQDGD SMATREELTA FLHPEEFPHM RDIVIAETLE DLDRNKDGYV QVEEYIADLY TAEPGEEEPA WVQTEREQFR DFRDLNKDGK LNGSEVGHWV LPPAQDQPLV EANHLLHESD TDKDGRLSKA EILGNWNMFV GSQATNYGED LTRHHDEL //