COPA1_MOUSE
ID COPA1_MOUSE Reviewed; 666 AA.
AC Q99MQ5; G3X9H6;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Collagen alpha-1(XXV) chain;
DE AltName: Full=CLAC-P;
DE Contains:
DE RecName: Full=Collagen-like Alzheimer amyloid plaque component;
DE Short=CLAC;
GN Name=Col25a1 {ECO:0000312|MGI:MGI:1924268};
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] {ECO:0000305, ECO:0000312|EMBL:AAK37475.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:AAK37475.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAK37475.1};
RX PubMed=11927537; DOI=10.1093/emboj/21.7.1524;
RA Hashimoto T., Wakabayashi T., Watanabe A., Kowa H., Hosoda R., Nakamura A.,
RA Kanazawa I., Arai T., Takio K., Mann D.M.A., Iwatsubo T.;
RT "CLAC: a novel Alzheimer amyloid plaque component derived from a
RT transmembrane precursor, CLAC-P/collagen type XXV.";
RL EMBO J. 21:1524-1534(2002).
RN [2]
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 [3]
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.
CC -!- FUNCTION: Inhibits fibrillization of amyloid-beta peptide during the
CC elongation phase. Has also been shown to assemble amyloid fibrils into
CC protease-resistant aggregates. Binds heparin (By similarity).
CC {ECO:0000250|UniProtKB:Q9BXS0}.
CC -!- SUBUNIT: Forms homodimers and homotrimers. Binds to the fibrillized
CC forms of amyloid-beta protein 40 (beta-APP40) and amyloid-betad protein
CC 42 (beta-APP42). Found associated with beta-APP42 more frequently than
CC with beta-APP40 (By similarity). {ECO:0000250|UniProtKB:Q9BXS0}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}. Note=After proteolytic cleavage, CLAC
CC is secreted. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in neurons with low levels
CC also detected in heart, testis and eye. {ECO:0000269|PubMed:11927537}.
CC -!- PTM: Undergoes proteolytic cleavage by furin protease to yield the
CC soluble collagen-like Alzheimer amyloid plaque component.
CC {ECO:0000250|UniProtKB:Q9BXS0}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q9BXS0}.
CC -!- PTM: Hydroxylated on proline and lysine residues.
CC {ECO:0000250|UniProtKB:Q9BXS0}.
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DR EMBL; AF315290; AAK37475.1; -; mRNA.
DR EMBL; AC091312; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC110540; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC114642; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC164078; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466532; EDL12220.1; -; Genomic_DNA.
DR CCDS; CCDS38637.1; -.
DR RefSeq; NP_084114.2; NM_029838.4.
DR AlphaFoldDB; Q99MQ5; -.
DR STRING; 10090.ENSMUSP00000079210; -.
DR iPTMnet; Q99MQ5; -.
DR PhosphoSitePlus; Q99MQ5; -.
DR PaxDb; Q99MQ5; -.
DR PRIDE; Q99MQ5; -.
DR ProteomicsDB; 284082; -.
DR Antibodypedia; 7049; 180 antibodies from 26 providers.
DR DNASU; 77018; -.
DR Ensembl; ENSMUST00000080335; ENSMUSP00000079210; ENSMUSG00000058897.
DR GeneID; 77018; -.
DR KEGG; mmu:77018; -.
DR UCSC; uc008riz.1; mouse.
DR CTD; 84570; -.
DR MGI; MGI:1924268; Col25a1.
DR VEuPathDB; HostDB:ENSMUSG00000058897; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000159823; -.
DR HOGENOM; CLU_001074_21_1_1; -.
DR InParanoid; Q99MQ5; -.
DR OrthoDB; 669310at2759; -.
DR PhylomeDB; Q99MQ5; -.
DR TreeFam; TF338175; -.
DR BioGRID-ORCS; 77018; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Col25a1; mouse.
DR PRO; PR:Q99MQ5; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q99MQ5; protein.
DR Bgee; ENSMUSG00000058897; Expressed in median eminence of neurohypophysis and 155 other tissues.
DR ExpressionAtlas; Q99MQ5; baseline and differential.
DR Genevisible; Q99MQ5; MM.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0001540; F:amyloid-beta binding; ISS:UniProtKB.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0060385; P:axonogenesis involved in innervation; IMP:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR InterPro; IPR008160; Collagen.
DR Pfam; PF01391; Collagen; 6.
PE 2: Evidence at transcript level;
KW Amyloid; Collagen; Glycoprotein; Heparin-binding; Hydroxylation; Membrane;
KW Reference proteome; Repeat; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..666
FT /note="Collagen alpha-1(XXV) chain"
FT /id="PRO_0000259613"
FT CHAIN 113..654
FT /note="Collagen-like Alzheimer amyloid plaque component"
FT /evidence="ECO:0000250|UniProtKB:Q9BXS0"
FT /id="PRO_0000259614"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..666
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 121..164
FT /note="Collagen-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 192..247
FT /note="Collagen-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 249..308
FT /note="Collagen-like 3"
FT /evidence="ECO:0000255"
FT DOMAIN 311..370
FT /note="Collagen-like 4"
FT /evidence="ECO:0000255"
FT DOMAIN 373..425
FT /note="Collagen-like 5"
FT /evidence="ECO:0000255"
FT DOMAIN 455..514
FT /note="Collagen-like 6"
FT /evidence="ECO:0000255"
FT DOMAIN 529..588
FT /note="Collagen-like 7"
FT /evidence="ECO:0000255"
FT DOMAIN 589..648
FT /note="Collagen-like 8"
FT /evidence="ECO:0000255"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..188
FT /note="Interaction with amyloid-beta peptide"
FT /evidence="ECO:0000250|UniProtKB:Q9BXS0"
FT REGION 189..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..210
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..547
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..634
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 112..113
FT /note="Cleavage; by furin"
FT /evidence="ECO:0000250"
FT CONFLICT 64
FT /note="A -> V (in Ref. 1; AAK37475)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="H -> Y (in Ref. 1; AAK37475)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="A -> V (in Ref. 1; AAK37475)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 666 AA; 65377 MW; DD8F5CAADE401366 CRC64;
MLVKKLAGKG GGRESGSEDP RPLGQRCAGT MPSCTALATL LSVVAVAFCF YLGVKTNDLQ
ARIAALESAK GTPSFHPLSD TVDELKAMVQ EKVERLLAQK SYEHMAKIRT AREAPLECNC
PAGPPGKRGK RGRRGESGPP GQPGPQGPPG PKGDKGEQGD QGPRMVFPKI NHGFLSADQQ
LIKRRLIKGD QGQAGPPGPP GPPGPRGPPG DTGKDGPRGM PGVPGEPGKP GEQGLMGPLG
PPGQKGSIGA PGTPGMDGQK GEPGSPGAAG QSGLPGPKGE PGKEGEKGDA GENGPKGDTG
EKGDPGSSAA GIKGEPGESG RPGQKGEPGL PGLPGLPGIK GEPGFIGPQG EPGLPGLPGT
KGDRGEAGPP GRGERGDPGA PGPKGKQGES GARGPKGSKG DRGDKGDSGA LGPRGPPGQK
GDPGATEIID YNGNLHEALQ RITTLTVTGP PGPPGPQGLQ GPKGEQGSPG IPGVDGEQGL
KGSKGDMGDP GVPGEKGGLG LPGLPGANGV KGEKGDTGLP GPQGPSIIGP PGPPGPHGPP
GPMGPHGLPG PKGASGLDGK PGSRGADGPI GPHGPAGPKG ERGEKGAMGE PGPRGPYGLP
GKDGEPGLDG FPGPRGEKGD LGEKGEKGFR GVKGEKGEPG QPGLDGLDAP CQLGPDGLPM
PGCWQK
