CAB45_RAT
ID CAB45_RAT Reviewed; 361 AA.
AC Q91ZS3; Q5PQW3;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=BDIX;
RX PubMed=18355758; DOI=10.1016/s1673-8527(08)60021-1;
RA Zhu Y., Wang Q., Xu W., Li S.;
RT "The ethanol response gene Cab45 can modulate the impairment elicited by
RT ethanol and ultraviolet in PC12 cells.";
RL J. Genet. Genomics 35:153-161(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Heart;
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 [3]
RP FUNCTION, INTERACTION WITH STXBP1, SUBCELLULAR LOCATION, AND TISSUE
RP 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-192, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: A membrane-associated isoform may be involved in the
CC exocytosis of zymogens by pancreatic acini. May regulate calcium-
CC dependent activities in the endoplasmic reticulum lumen or post-ER
CC compartment. {ECO:0000269|PubMed:17442889}.
CC -!- SUBUNIT: A membrane-associated isoform interacts with STX3 and STXBP1.
CC {ECO:0000269|PubMed:17442889}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus lumen
CC {ECO:0000250|UniProtKB:Q61112}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q91ZS3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91ZS3-2; Sequence=VSP_037452;
CC -!- TISSUE SPECIFICITY: A membrane-associated isoform is expressed in acini
CC of the pancreas (at protein level). Ubiquitous.
CC {ECO:0000269|PubMed:17442889, ECO:0000269|PubMed:18355758}.
CC -!- INDUCTION: Down-regulated by ethanol. Down-regulated during the
CC progression of cerebellum differentiation.
CC {ECO:0000269|PubMed:18355758}.
CC -!- DOMAIN: Binds calcium via its EF-hands. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CREC family. {ECO:0000305}.
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DR EMBL; AF405545; AAL01370.1; -; mRNA.
DR EMBL; BC086996; AAH86996.1; -; mRNA.
DR RefSeq; NP_569096.2; NM_130412.2.
DR AlphaFoldDB; Q91ZS3; -.
DR STRING; 10116.ENSRNOP00000027215; -.
DR GlyGen; Q91ZS3; 1 site.
DR iPTMnet; Q91ZS3; -.
DR PhosphoSitePlus; Q91ZS3; -.
DR jPOST; Q91ZS3; -.
DR PaxDb; Q91ZS3; -.
DR PRIDE; Q91ZS3; -.
DR GeneID; 155173; -.
DR KEGG; rno:155173; -.
DR CTD; 51150; -.
DR RGD; 621521; Sdf4.
DR eggNOG; KOG4251; Eukaryota.
DR InParanoid; Q91ZS3; -.
DR OrthoDB; 1156280at2759; -.
DR PhylomeDB; Q91ZS3; -.
DR TreeFam; TF314849; -.
DR PRO; PR:Q91ZS3; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005796; C:Golgi lumen; ISS:BHF-UCL.
DR GO; GO:0005770; C:late endosome; IDA:BHF-UCL.
DR GO; GO:0005509; F:calcium ion binding; ISS:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:BHF-UCL.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; IMP:BHF-UCL.
DR GO; GO:0021549; P:cerebellum development; IEP:BHF-UCL.
DR GO; GO:0045444; P:fat cell differentiation; ISS:BHF-UCL.
DR GO; GO:0099558; P:maintenance of synapse structure; ISO:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:BHF-UCL.
DR GO; GO:0009650; P:UV protection; IMP:BHF-UCL.
DR GO; GO:0070625; P:zymogen granule exocytosis; IMP: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; Exocytosis; 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_0000004158"
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 /evidence="ECO:0000250"
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:0007744|PubMed:22673903"
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 1
FT /note="M -> MTSRAPNCAPQTRRIRKPGSPV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037452"
FT CONFLICT 5
FT /note="V -> A (in Ref. 2; AAH86996)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 361 AA; 42075 MW; 1BF74F014B033FC5 CRC64;
MVWLVAMTSR QRSLCGLAAH GLWFLGLVLL MDATARPANH SFSRERAANR DENEIIPPDH
LNGVKLEMDG HLNKDFHQEV FLGKDMDGFD EDSEPRRSRR KLMVIFSKVD VNTDRRISAK
EMQHWIMEKT AEHFQEAVKE NKLHFRAVDP DGDGHVSWDE YKVKFLASKG HNEREIADAI
KNHEELKVDE ETQEVLGNLR DRWYQADNPP ADLLLTEDEF LSFLHPEHSR GMLKFMVKEI
VRDLDQDGDK QLSLPEFISL PVGTVENQQG QDIDDNWVKD RKKEFEELID SNHDGIVTME
ELENYMDPMN EYNALNEAKQ MIAIADENQN HHLEPEEILK YSEFFTGSKL MDYARNVHEE
F
