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   24-JAN-2024, entry version 141.
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; 10090-ENSMUSP00000079210; -.
DR   ProteomicsDB; 284082; -.
DR   Antibodypedia; 7049; 210 antibodies from 26 providers.
DR   DNASU; 77018; -.
DR   Ensembl; ENSMUST00000080335.11; ENSMUSP00000079210.5; ENSMUSG00000058897.19.
DR   GeneID; 77018; -.
DR   KEGG; mmu:77018; -.
DR   UCSC; uc008riz.1; mouse.
DR   AGR; MGI:1924268; -.
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; 5362873at2759; -.
DR   PhylomeDB; Q99MQ5; -.
DR   TreeFam; TF338175; -.
DR   Reactome; R-MMU-1442490; Collagen degradation.
DR   Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR   Reactome; R-MMU-8948216; Collagen chain trimerization.
DR   BioGRID-ORCS; 77018; 3 hits in 77 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 156 other cell types or tissues.
DR   ExpressionAtlas; Q99MQ5; baseline and differential.
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:0005576; C:extracellular region; ISO:MGI.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0001540; F:amyloid-beta binding; ISS:UniProtKB.
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   InterPro; IPR008160; Collagen.
DR   PANTHER; PTHR37456:SF3; COLLAGEN ALPHA-1(XXV) CHAIN; 1.
DR   PANTHER; PTHR37456; SI:CH211-266K2.1; 1.
DR   Pfam; PF01391; Collagen; 6.
DR   Genevisible; Q99MQ5; MM.
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
//