CAB45_HUMAN
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 03-AUG-2022, entry version 192.
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};
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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_057260.2; NM_016176.3.
DR RefSeq; NP_057260.3; NM_016176.6.
DR RefSeq; NP_057631.1; NM_016547.2.
DR RefSeq; XP_011539858.1; XM_011541556.1. [Q9BRK5-4]
DR AlphaFoldDB; Q9BRK5; -.
DR BioGRID; 119334; 139.
DR IntAct; Q9BRK5; 96.
DR MINT; Q9BRK5; -.
DR STRING; 9606.ENSP00000353094; -.
DR TCDB; 8.A.82.3.1; the calmodulin calcium binding protein (calmodulin) family.
DR GlyGen; Q9BRK5; 3 sites, 1 O-linked glycan (1 site).
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; Q9BRK5; -.
DR PeptideAtlas; Q9BRK5; -.
DR PRIDE; 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 TopDownProteomics; Q9BRK5-4; -. [Q9BRK5-4]
DR Antibodypedia; 26159; 291 antibodies from 31 providers.
DR DNASU; 51150; -.
DR Ensembl; ENST00000660930.1; ENSP00000499296.1; ENSG00000078808.19. [Q9BRK5-6]
DR GeneID; 51150; -.
DR KEGG; hsa:51150; -.
DR UCSC; uc001adh.5; human. [Q9BRK5-1]
DR CTD; 51150; -.
DR DisGeNET; 51150; -.
DR GeneCards; SDF4; -.
DR HGNC; HGNC:24188; SDF4.
DR HPA; ENSG00000078808; Low tissue specificity.
DR MIM; 614282; gene.
DR neXtProt; NX_Q9BRK5; -.
DR OpenTargets; ENSG00000078808; -.
DR PharmGKB; PA142670940; -.
DR VEuPathDB; HostDB:ENSG00000078808; -.
DR eggNOG; KOG4251; Eukaryota.
DR GeneTree; ENSGT01010000222360; -.
DR HOGENOM; CLU_044718_1_0_1; -.
DR InParanoid; Q9BRK5; -.
DR OrthoDB; 1156280at2759; -.
DR PhylomeDB; Q9BRK5; -.
DR TreeFam; TF314849; -.
DR PathwayCommons; Q9BRK5; -.
DR SignaLink; Q9BRK5; -.
DR BioGRID-ORCS; 51150; 6 hits in 1079 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 192 other tissues.
DR ExpressionAtlas; Q9BRK5; baseline and differential.
DR Genevisible; Q9BRK5; HS.
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:0005794; C:Golgi apparatus; IDA:HPA.
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 InterPro; IPR027240; CAB45.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR PANTHER; PTHR10827:SF51; PTHR10827:SF51; 1.
DR Pfam; PF13202; EF-hand_5; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 5.
DR SUPFAM; SSF47473; SSF47473; 2.
DR PROSITE; PS00018; EF_HAND_1; 5.
DR PROSITE; PS50222; EF_HAND_2; 5.
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
