ID CAB45_HUMAN Reviewed; 362 AA. AC Q9BRK5; B1AME5; B1AME6; B2RDF1; B4DSM1; Q53G52; Q53HQ9; Q8NBQ3; Q96AA1; AC Q9NZP7; Q9UN53; DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 27-MAR-2024, entry version 201. DE RecName: Full=45 kDa calcium-binding protein; DE Short=Cab45; DE AltName: Full=Stromal cell-derived factor 4; DE Short=SDF-4; DE Flags: Precursor; GN Name=SDF4; Synonyms=CAB45; ORFNames=PSEC0034; 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 6). RX PubMed=9254016; DOI=10.3109/10425179709034038; RA Koivu T., Laitinen S., Riento K., Olkkonen V.M.; RT "Sequence of a human cDNA encoding Cab45, a Ca2+-binding protein with six RT EF-hand motifs."; RL DNA Seq. 7:217-220(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Yue P., Yu L., Zhao S.Y.; RT "Cloning of a new human cDNA homologous to Mus musculus calcium-binding RT protein Cab45b."; RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RA Zhang W., Wan T., Yuan Z., Cao X.; RT "Novel human calcium-binding protein precursor."; RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Zhang W., Wan T., Cao X.; RT "Identification of a novel calcium-binding protein Cab45 from dendritic RT cells."; RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4). RC TISSUE=Brain, and Tongue; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Teratocarcinoma; RX PubMed=16303743; DOI=10.1093/dnares/12.2.117; RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y., RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., RA Isogai T.; RT "Signal sequence and keyword trap in silico for selection of full-length RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA RT libraries."; RL DNA Res. 12:117-126(2005). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Adipose tissue; 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.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 [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain, Pancreas, and Prostate; 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 [11] RP INTERACTION WITH STX3 AND STXBP1, SUBCELLULAR LOCATION, ALTERNATIVE RP SPLICING (ISOFORM 5), MUTAGENESIS OF GLU-257; GLU-302 AND GLU-338, AND RP TISSUE SPECIFICITY. RX PubMed=17442889; DOI=10.1091/mbc.e06-10-0950; RA Lam P.P., Hyvaerinen K., Kauppi M., Cosen-Binker L., Laitinen S., RA Keraenen S., Gaisano H.Y., Olkkonen V.M.; RT "A cytosolic splice variant of Cab45 interacts with Munc18b and impacts on RT amylase secretion by pancreatic acini."; RL Mol. Biol. Cell 18:2473-2480(2007). RN [12] 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-193; THR-217; THR-265 AND RP THR-299, AND 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 [15] RP VARIANT [LARGE SCALE ANALYSIS] THR-148. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: May regulate calcium-dependent activities in the endoplasmic CC reticulum lumen or post-ER compartment. {ECO:0000250}. CC -!- FUNCTION: Isoform 5 may be involved in the exocytosis of zymogens by CC pancreatic acini. CC -!- SUBUNIT: Isoform 5 interacts with STXBP1; the interaction is enhanced CC in presence of calcium. Isoform 5 interacts with STX3. CC {ECO:0000269|PubMed:17442889}. CC -!- INTERACTION: CC Q9BRK5; P55212: CASP6; NbExp=3; IntAct=EBI-1389808, EBI-718729; CC Q9BRK5; P13473-2: LAMP2; NbExp=3; IntAct=EBI-1389808, EBI-21591415; CC Q9BRK5; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-1389808, EBI-5280197; CC Q9BRK5; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-1389808, EBI-2623095; CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Golgi apparatus lumen CC {ECO:0000250|UniProtKB:Q61112}. CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm CC {ECO:0000269|PubMed:17442889}. Cell membrane CC {ECO:0000269|PubMed:17442889}. Cell projection, bleb. Note=Isoform 5 CC colocalizes with STX3 and STXBP1 isoform 2 at the plasma membrane and CC cell surface blebs. {ECO:0000269|PubMed:17442889}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; Synonyms=Cab45a, Cab45-G; CC IsoId=Q9BRK5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9BRK5-2; Sequence=VSP_037485; CC Name=3; CC IsoId=Q9BRK5-3; Sequence=VSP_037486, VSP_037489; CC Name=4; CC IsoId=Q9BRK5-4; Sequence=VSP_037487, VSP_037488; CC Name=5; Synonyms=Cab45b, Cab45-C; CC IsoId=Q9BRK5-5; Sequence=VSP_037484; CC Name=6; CC IsoId=Q9BRK5-6; Sequence=VSP_040559; CC -!- TISSUE SPECIFICITY: Ubiquitous. Isoform 5 is expressed in pancreas. CC {ECO:0000269|PubMed:17442889}. CC -!- DOMAIN: Binds calcium via its EF-hands (By similarity). Isoform 5 binds CC calcium. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the CREC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAL75950.1; Type=Frameshift; Evidence={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; L79912; AAL40084.1; -; mRNA. DR EMBL; AF132749; AAL75950.1; ALT_FRAME; mRNA. DR EMBL; AF153686; AAD51612.1; -; mRNA. DR EMBL; AF178986; AAF44350.1; -; mRNA. DR EMBL; AK027277; BAB55012.1; -; mRNA. DR EMBL; AK299810; BAG61683.1; -; mRNA. DR EMBL; AK315517; BAG37898.1; -; mRNA. DR EMBL; AK075352; BAC11563.1; -; mRNA. DR EMBL; AK222521; BAD96241.1; -; mRNA. DR EMBL; AK223079; BAD96799.1; -; mRNA. DR EMBL; AL162741; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471183; EAW56272.1; -; Genomic_DNA. DR EMBL; CH471183; EAW56273.1; -; Genomic_DNA. DR EMBL; BC006211; AAH06211.1; -; mRNA. DR EMBL; BC007625; AAH07625.1; -; mRNA. DR EMBL; BC008917; AAH08917.1; -; mRNA. DR EMBL; BC011244; AAH11244.1; -; mRNA. DR EMBL; BC022375; AAH22375.1; -; mRNA. DR RefSeq; NP_057631.1; NM_016547.2. DR RefSeq; XP_011539858.1; XM_011541556.1. [Q9BRK5-4] DR AlphaFoldDB; Q9BRK5; -. DR BioGRID; 119334; 159. DR IntAct; Q9BRK5; 100. DR MINT; Q9BRK5; -. DR STRING; 9606.ENSP00000499387; -. DR TCDB; 8.A.82.3.1; the calmodulin calcium binding protein (calmodulin) family. DR GlyCosmos; Q9BRK5; 2 sites, 1 glycan. DR GlyGen; Q9BRK5; 9 sites, 2 O-linked glycans (7 sites). DR iPTMnet; Q9BRK5; -. DR MetOSite; Q9BRK5; -. DR PhosphoSitePlus; Q9BRK5; -. DR BioMuta; SDF4; -. DR DMDM; 21263447; -. DR EPD; Q9BRK5; -. DR jPOST; Q9BRK5; -. DR MassIVE; Q9BRK5; -. DR MaxQB; Q9BRK5; -. DR PaxDb; 9606-ENSP00000353094; -. DR PeptideAtlas; Q9BRK5; -. DR ProteomicsDB; 78779; -. [Q9BRK5-1] DR ProteomicsDB; 78780; -. [Q9BRK5-2] DR ProteomicsDB; 78781; -. [Q9BRK5-3] DR ProteomicsDB; 78782; -. [Q9BRK5-4] DR ProteomicsDB; 78783; -. [Q9BRK5-5] DR ProteomicsDB; 78784; -. [Q9BRK5-6] DR Pumba; Q9BRK5; -. DR TopDownProteomics; Q9BRK5-4; -. [Q9BRK5-4] DR Antibodypedia; 26159; 314 antibodies from 31 providers. DR DNASU; 51150; -. DR GeneID; 51150; -. DR KEGG; hsa:51150; -. DR UCSC; uc001adh.5; human. [Q9BRK5-1] DR AGR; HGNC:24188; -. DR CTD; 51150; -. DR DisGeNET; 51150; -. DR GeneCards; SDF4; -. DR HGNC; HGNC:24188; SDF4. DR MIM; 614282; gene. DR neXtProt; NX_Q9BRK5; -. DR PharmGKB; PA142670940; -. DR VEuPathDB; HostDB:ENSG00000078808; -. DR eggNOG; KOG4251; Eukaryota. DR HOGENOM; CLU_044718_1_0_1; -. DR InParanoid; Q9BRK5; -. DR OrthoDB; 2913938at2759; -. DR PhylomeDB; Q9BRK5; -. DR TreeFam; TF314849; -. DR PathwayCommons; Q9BRK5; -. DR SignaLink; Q9BRK5; -. DR BioGRID-ORCS; 51150; 6 hits in 1154 CRISPR screens. DR ChiTaRS; SDF4; human. DR GeneWiki; SDF4; -. DR GenomeRNAi; 51150; -. DR Pharos; Q9BRK5; Tbio. DR PRO; PR:Q9BRK5; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9BRK5; Protein. DR Bgee; ENSG00000078808; Expressed in stromal cell of endometrium and 193 other cell types or tissues. DR ExpressionAtlas; Q9BRK5; baseline and differential. DR GO; GO:0032059; C:bleb; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL. DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005796; C:Golgi lumen; ISS:BHF-UCL. DR GO; GO:0005770; C:late endosome; ISS:BHF-UCL. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005509; F:calcium ion binding; IDA:BHF-UCL. DR GO; GO:0042802; F:identical protein binding; ISS:BHF-UCL. DR GO; GO:0017156; P:calcium-ion regulated exocytosis; ISS:BHF-UCL. DR GO; GO:0021549; P:cerebellum development; ISS:BHF-UCL. DR GO; GO:0045444; P:fat cell differentiation; ISS:BHF-UCL. DR GO; GO:0099558; P:maintenance of synapse structure; IGI:FlyBase. DR GO; GO:0045471; P:response to ethanol; ISS:BHF-UCL. DR GO; GO:0009650; P:UV protection; ISS:BHF-UCL. DR GO; GO:0070625; P:zymogen granule exocytosis; ISS:BHF-UCL. DR CDD; cd16225; EFh_CREC_cab45; 1. DR Gene3D; 1.10.238.10; EF-hand; 2. DR InterPro; IPR027240; CAB45_EFh. DR InterPro; IPR011992; EF-hand-dom_pair. DR InterPro; IPR018247; EF_Hand_1_Ca_BS. DR InterPro; IPR002048; EF_hand_dom. DR PANTHER; PTHR10827:SF98; 45 KDA CALCIUM-BINDING PROTEIN; 1. DR PANTHER; PTHR10827; RETICULOCALBIN; 1. DR Pfam; PF13202; EF-hand_5; 1. DR Pfam; PF13499; EF-hand_7; 1. 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; Q9BRK5; HS. PE 1: Evidence at protein level; KW Alternative splicing; Calcium; Cell membrane; Cell projection; Cytoplasm; KW Exocytosis; Glycoprotein; Golgi apparatus; Membrane; Metal-binding; KW Phosphoprotein; Reference proteome; Repeat; Signal. FT SIGNAL 1..36 FT /evidence="ECO:0000255" FT CHAIN 37..362 FT /note="45 kDa calcium-binding protein" FT /id="PRO_0000004156" FT DOMAIN 98..133 FT /note="EF-hand 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 137..172 FT /note="EF-hand 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 197..232 FT /note="EF-hand 3" FT /evidence="ECO:0000305" FT DOMAIN 233..268 FT /note="EF-hand 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 278..313 FT /note="EF-hand 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 314..349 FT /note="EF-hand 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT REGION 309..362 FT /note="Necessary for intracellular retention in Golgi FT apparatus lumen" FT /evidence="ECO:0000250" FT BINDING 111 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 113 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 115 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 117 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 122 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 150 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 152 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 154 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 156 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 161 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 213 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000305" FT BINDING 220 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000305" FT BINDING 246 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 248 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 250 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 252 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 257 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 291 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 293 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 295 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 302 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 327 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 329 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 331 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 333 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 338 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT MOD_RES 99 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 193 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 217 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 265 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 299 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT CARBOHYD 40 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 1..232 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000305" FT /id="VSP_037484" FT VAR_SEQ 1..103 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_037485" FT VAR_SEQ 193..254 FT /note="TQEVLENLKDRWYQADSPPADLLLTEEEFLSFLHPEHSRGMLRFMVKEIVRD FT LDQDGDKQLS -> SCAPLSTGSPGEPEGPLVPGGQPPCRPAADGGGVPVGPPPRAQPG FT NAQVHGEGDRPGPGPGR (in isoform 3)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_037486" FT VAR_SEQ 193..202 FT /note="TQEVLENLKD -> RHGPPGPRAL (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_037487" FT VAR_SEQ 203..362 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_037488" FT VAR_SEQ 255..362 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_037489" FT VAR_SEQ 305..362 FT /note="SYMDPMNEYNALNEAKQMIAVADENQNHHLEPEEVLKYSEFFTGSKLVDYAR FT SVHEEF -> NVPTLPLQPIGTLNSHFVRLAAELGGGKATLTCAPLARRATWTP (in FT isoform 6)" FT /evidence="ECO:0000303|PubMed:9254016" FT /id="VSP_040559" FT VARIANT 50 FT /note="N -> D (in dbSNP:rs12745364)" FT /id="VAR_048659" FT VARIANT 148 FT /note="A -> T (in a colorectal cancer sample; somatic FT mutation; dbSNP:rs766752243)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035461" FT MUTAGEN 257 FT /note="E->Q: Does not affect calcium-binding." FT /evidence="ECO:0000269|PubMed:17442889" FT MUTAGEN 302 FT /note="E->Q: Inhibits calcium-binding." FT /evidence="ECO:0000269|PubMed:17442889" FT MUTAGEN 338 FT /note="E->Q: Does not affect calcium-binding." FT /evidence="ECO:0000269|PubMed:17442889" FT CONFLICT 78 FT /note="H -> Q (in Ref. 2; AAL75950)" FT /evidence="ECO:0000305" FT CONFLICT 86 FT /note="D -> N (in Ref. 2; AAL75950)" FT /evidence="ECO:0000305" FT CONFLICT 89 FT /note="G -> C (in Ref. 2; AAL75950)" FT /evidence="ECO:0000305" FT CONFLICT 92 FT /note="E -> R (in Ref. 2; AAL75950)" FT /evidence="ECO:0000305" FT CONFLICT 94 FT /note="A -> T (in Ref. 2; AAL75950)" FT /evidence="ECO:0000305" FT CONFLICT 97 FT /note="R -> P (in Ref. 2; AAL75950)" FT /evidence="ECO:0000305" FT CONFLICT 117 FT /note="K -> R (in Ref. 6; BAC11563)" FT /evidence="ECO:0000305" FT CONFLICT 133 FT /note="E -> G (in Ref. 6; BAC11563)" FT /evidence="ECO:0000305" FT CONFLICT 150 FT /note="D -> G (in Ref. 2; AAL75950)" FT /evidence="ECO:0000305" FT CONFLICT 188 FT /note="K -> R (in Ref. 5; BAG37898)" FT /evidence="ECO:0000305" FT CONFLICT 193 FT /note="T -> A (in Ref. 7; BAD96241)" FT /evidence="ECO:0000305" FT CONFLICT 234 FT /note="L -> P (in Ref. 7; BAD96799)" FT /evidence="ECO:0000305" FT CONFLICT 281..282 FT /note="DR -> KK (in Ref. 2; AAL75950)" FT /evidence="ECO:0000305" FT CONFLICT 286 FT /note="F -> L (in Ref. 2; AAL75950)" FT /evidence="ECO:0000305" FT CONFLICT 321 FT /note="Q -> R (in Ref. 7; BAD96799)" FT /evidence="ECO:0000305" FT CONFLICT 356 FT /note="R -> S (in Ref. 2; AAL75950)" FT /evidence="ECO:0000305" SQ SEQUENCE 362 AA; 41807 MW; 440C6990149AAE2C CRC64; MVWPWVAMAS RWGPLIGLAP CCLWLLGAVL LMDASARPAN HSSTRERVAN REENEILPPD HLNGVKLEMD GHLNRGFHQE VFLGKDLGGF DEDAEPRRSR RKLMVIFSKV DVNTDRKISA KEMQRWIMEK TAEHFQEAME ESKTHFRAVD PDGDGHVSWD EYKVKFLASK GHSEKEVADA IRLNEELKVD EETQEVLENL KDRWYQADSP PADLLLTEEE FLSFLHPEHS RGMLRFMVKE IVRDLDQDGD KQLSVPEFIS LPVGTVENQQ GQDIDDNWVK DRKKEFEELI DSNHDGIVTA EELESYMDPM NEYNALNEAK QMIAVADENQ NHHLEPEEVL KYSEFFTGSK LVDYARSVHE EF //