CAB45_MOUSE
ID CAB45_MOUSE Reviewed; 361 AA.
AC Q61112; Q3TK84; Q3TQP8; Q61113;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 157.
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;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANT
RP LYS-281.
RX PubMed=8609160; DOI=10.1083/jcb.133.2.257;
RA Scherer P.E., Lederkremer G.Z., Williams S., Fogliano M., Baldini G.,
RA Lodish H.F.;
RT "Cab45, a novel (Ca2+)-binding protein localized to the Golgi lumen.";
RL J. Cell Biol. 133:257-268(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8938438; DOI=10.1006/geno.1996.0560;
RA Shirozu M., Tada H., Tashiro K., Nakamura T., Lopez N.D., Nazarea M.,
RA Hamada T., Sato T., Nakano T., Honjo T.;
RT "Characterization of novel secreted and membrane proteins isolated by the
RT signal sequence trap method.";
RL Genomics 37:273-280(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Egg;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [7]
RP SUBCELLULAR LOCATION.
RX PubMed=16608874; DOI=10.1242/jcs.02905;
RA Lara-Lemus R., Liu M., Turner M.D., Scherer P., Stenbeck G., Iyengar P.,
RA Arvan P.;
RT "Lumenal protein sorting to the constitutive secretory pathway of a
RT regulated secretory cell.";
RL J. Cell Sci. 119:1833-1842(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Pancreas, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May regulate calcium-dependent activities in the endoplasmic
CC reticulum lumen or post-ER compartment.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus lumen
CC {ECO:0000269|PubMed:16608874}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q61112-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q61112-2; Sequence=VSP_037450, VSP_037451;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:8609160}.
CC -!- DOMAIN: Binds calcium, probably via its EF-hands.
CC -!- SIMILARITY: Belongs to the CREC family. {ECO:0000305}.
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DR EMBL; U45977; AAB01812.1; -; mRNA.
DR EMBL; U45978; AAB01813.1; -; mRNA.
DR EMBL; D50461; BAA09052.1; -; mRNA.
DR EMBL; AK157860; BAE34238.1; -; mRNA.
DR EMBL; AK163400; BAE37334.1; -; mRNA.
DR EMBL; AK167113; BAE39261.1; -; mRNA.
DR EMBL; AL627204; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466594; EDL15066.1; -; Genomic_DNA.
DR EMBL; BC068152; AAH68152.1; -; mRNA.
DR CCDS; CCDS19054.1; -. [Q61112-1]
DR CCDS; CCDS80198.1; -. [Q61112-2]
DR RefSeq; NP_001289396.1; NM_001302467.1. [Q61112-1]
DR RefSeq; NP_001289397.1; NM_001302468.1. [Q61112-1]
DR RefSeq; NP_001289398.1; NM_001302469.1. [Q61112-2]
DR RefSeq; NP_035471.1; NM_011341.5. [Q61112-1]
DR AlphaFoldDB; Q61112; -.
DR BioGRID; 203141; 3.
DR STRING; 10090.ENSMUSP00000053175; -.
DR GlyGen; Q61112; 1 site.
DR iPTMnet; Q61112; -.
DR PhosphoSitePlus; Q61112; -.
DR EPD; Q61112; -.
DR jPOST; Q61112; -.
DR MaxQB; Q61112; -.
DR PaxDb; Q61112; -.
DR PeptideAtlas; Q61112; -.
DR PRIDE; Q61112; -.
DR ProteomicsDB; 273569; -. [Q61112-1]
DR ProteomicsDB; 273570; -. [Q61112-2]
DR Antibodypedia; 26159; 291 antibodies from 31 providers.
DR DNASU; 20318; -.
DR Ensembl; ENSMUST00000050078; ENSMUSP00000053175; ENSMUSG00000029076. [Q61112-1]
DR Ensembl; ENSMUST00000097734; ENSMUSP00000095340; ENSMUSG00000029076. [Q61112-2]
DR Ensembl; ENSMUST00000105578; ENSMUSP00000101203; ENSMUSG00000029076. [Q61112-1]
DR Ensembl; ENSMUST00000105579; ENSMUSP00000101204; ENSMUSG00000029076. [Q61112-1]
DR GeneID; 20318; -.
DR KEGG; mmu:20318; -.
DR UCSC; uc008wfr.2; mouse. [Q61112-1]
DR UCSC; uc056zys.1; mouse. [Q61112-2]
DR CTD; 51150; -.
DR MGI; MGI:108079; Sdf4.
DR VEuPathDB; HostDB:ENSMUSG00000029076; -.
DR eggNOG; KOG4251; Eukaryota.
DR GeneTree; ENSGT01010000222360; -.
DR HOGENOM; CLU_044718_1_0_1; -.
DR InParanoid; Q61112; -.
DR OMA; QYINRRI; -.
DR OrthoDB; 1156280at2759; -.
DR PhylomeDB; Q61112; -.
DR TreeFam; TF314849; -.
DR BioGRID-ORCS; 20318; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Sdf4; mouse.
DR PRO; PR:Q61112; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q61112; protein.
DR Bgee; ENSMUSG00000029076; Expressed in stroma of bone marrow and 238 other tissues.
DR Genevisible; Q61112; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005796; C:Golgi lumen; IDA:BHF-UCL.
DR GO; GO:0005770; C:late endosome; IMP:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; ISO:MGI.
DR GO; GO:0021549; P:cerebellum development; ISS:BHF-UCL.
DR GO; GO:0045444; P:fat cell differentiation; IEP:BHF-UCL.
DR GO; GO:0099558; P:maintenance of synapse structure; ISO:MGI.
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; ISO:MGI.
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; Glycoprotein; Golgi apparatus;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Signal.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..361
FT /note="45 kDa calcium-binding protein"
FT /id="PRO_0000004157"
FT DOMAIN 97..132
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 136..171
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 196..231
FT /note="EF-hand 3"
FT /evidence="ECO:0000305"
FT DOMAIN 232..267
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 277..312
FT /note="EF-hand 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 313..348
FT /note="EF-hand 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 308..361
FT /note="Necessary for intracellular retention in Golgi
FT apparatus lumen"
FT BINDING 110
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 112
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 114
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 116
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 121
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 149
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 151
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 155
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 160
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000305"
FT BINDING 219
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000305"
FT BINDING 245
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 247
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 249
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 251
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 256
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 290
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 292
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 294
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 301
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 326
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 328
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 330
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 332
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 337
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRK5"
FT MOD_RES 192
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRK5"
FT MOD_RES 216
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRK5"
FT MOD_RES 264
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRK5"
FT MOD_RES 298
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRK5"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 192..218
FT /note="TQEVLGNLRDRWYQADNPPADLLLTED -> IALHFLLLTGGPLSCSSGETS
FT ICLSRL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_037450"
FT VAR_SEQ 219..361
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_037451"
FT VARIANT 281
FT /note="R -> K (in CAB45A)"
FT /evidence="ECO:0000269|PubMed:8609160"
SQ SEQUENCE 361 AA; 42064 MW; 2599E99F5F81A913 CRC64;
MVWLVAMTPR QSSLCGLAAH GLWFLGLVLL MDATARPANH SSTRERAANR EENEIMPPDH
LNGVKLEMDG HLNKDFHQEV FLGKDMDGFD EDSEPRRSRR KLMVIFSKVD VNTDRRISAK
EMQHWIMEKT AEHFQEAVKE NKLHFRAVDP DGDGHVSWDE YKVKFLASKG HNEREIAEAI
KNHEELKVDE ETQEVLGNLR DRWYQADNPP ADLLLTEDEF LSFLHPEHSR GMLKFMVKEI
FRDLDQDGDK QLSLPEFISL PVGTVENQQG QDIDDNWVKD RKKEFEELID SNHDGIVTME
ELENYMDPMN EYNALNEAKQ MIAIADENQN HHLEPEEILK YSEFFTGSKL MDYARNVHEE
F
