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Collagen alpha-1(XXV) chain (Alzheimer disease amyloid-associated protein) (AMY) (CLAC-P) [Cleaved into: Collagen-like Alzheimer amyloid plaque component (CLAC)]

 COPA1_HUMAN             Reviewed;         654 AA.
Q9BXS0; A8MPZ6; Q9BXR9;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 2.
18-JUL-2018, entry version 130.
RecName: Full=Collagen alpha-1(XXV) chain;
AltName: Full=Alzheimer disease amyloid-associated protein;
Short=AMY;
AltName: Full=CLAC-P;
Contains:
RecName: Full=Collagen-like Alzheimer amyloid plaque component;
Short=CLAC;
Name=COL25A1 {ECO:0000312|HGNC:HGNC:18603};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305, ECO:0000312|EMBL:AAK35008.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF
131-152 AND 156-214, INTERACTION WITH AMYLOID-BETA PEPTIDE, TISSUE
SPECIFICITY, CLEAVAGE, HYDROXYLATION, PYROGLUTAMATE FORMATION AT
GLU-113, AND MUTAGENESIS OF ARG-109 AND ARG-112.
PubMed=11927537; DOI=10.1093/emboj/21.7.1524;
Hashimoto T., Wakabayashi T., Watanabe A., Kowa H., Hosoda R.,
Nakamura A., Kanazawa I., Arai T., Takio K., Mann D.M.A., Iwatsubo T.;
"CLAC: a novel Alzheimer amyloid plaque component derived from a
transmembrane precursor, CLAC-P/collagen type XXV.";
EMBO J. 21:1524-1534(2002).
[2] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
PubMed=14656069; DOI=10.1093/jnen/62.11.1108;
Soederberg L., Zhukareva V., Bogdanovic N., Hashimoto T., Winblad B.,
Iwatsubo T., Lee V.M.Y., Trojanowski J.Q., Naeslund J.;
"Molecular identification of AMY, an Alzheimer disease amyloid-
associated protein.";
J. Neuropathol. Exp. Neurol. 62:1108-1117(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4] {ECO:0000305}
PROTEIN SEQUENCE OF CLAC N-TERMINUS, PROTEIN SEQUENCE OF 182-191 AND
445-452, FUNCTION, SUBUNIT, INTERACTION WITH AMYLOID-BETA PEPTIDE,
GLYCOSYLATION, HYDROXYLATION, AND MUTAGENESIS OF 181-LEU--LYS-188.
PubMed=15522881; DOI=10.1074/jbc.M403628200;
Soederberg L., Kakuyama H., Moeller A., Ito A., Winblad B.,
Tjernberg L.O., Naeslund J.;
"Characterization of the Alzheimer's disease-associated CLAC protein
and identification of an amyloid beta-peptide-binding site.";
J. Biol. Chem. 280:1007-1015(2005).
[5] {ECO:0000305}
INTERACTION WITH AMYLOID-BETA PEPTIDE.
PubMed=15215182; DOI=10.1016/S0002-9440(10)63295-6;
Kowa H., Sakakura T., Matsuura Y., Wakabayashi T., Mann D.M.A.,
Duff K., Tsuji S., Hashimoto T., Iwatsubo T.;
"Mostly separate distributions of CLAC- versus Abeta40- or thioflavin
S-reactivities in senile plaques reveal two distinct subpopulations of
beta-amyloid deposits.";
Am. J. Pathol. 165:273-281(2004).
[6] {ECO:0000305}
FUNCTION.
PubMed=16300410; DOI=10.1021/bi051263e;
Kakuyama H., Soederberg L., Horigome K., Winblad B., Dahlqvist C.,
Naeslund J., Tjernberg L.O.;
"CLAC binds to aggregated Abeta and Abeta fragments, and attenuates
fibril elongation.";
Biochemistry 44:15602-15609(2005).
[7] {ECO:0000305}
FUNCTION.
PubMed=15853808; DOI=10.1111/j.1742-4658.2005.04647.x;
Soederberg L., Dahlqvist C., Kakuyama H., Thyberg J., Ito A.,
Winblad B., Naeslund J., Tjernberg L.O.;
"Collagenous Alzheimer amyloid plaque component assembles amyloid
fibrils into protease resistant aggregates.";
FEBS J. 272:2231-2236(2005).
[8] {ECO:0000305}
FUNCTION, AND INTERACTION WITH AMYLOID-BETA PEPTIDE.
PubMed=15615705; DOI=10.1074/jbc.M413340200;
Osada Y., Hashimoto T., Nishimura A., Matsuo Y., Wakabayashi T.,
Iwatsubo T.;
"CLAC binds to amyloid beta peptides through the positively charged
amino acid cluster within the collagenous domain 1 and inhibits
formation of amyloid fibrils.";
J. Biol. Chem. 280:8596-8605(2005).
[9]
ERRATUM.
Osada Y., Hashimoto T., Nishimura A., Matsuo Y., Wakabayashi T.,
Iwatsubo T.;
J. Biol. Chem. 280:15484-15484(2005).
[10]
INVOLVEMENT IN CFEOM5, VARIANT CFEOM5 ARG-382, AND CHARACTERIZATION OF
VARIANT CFEOM5 ARG-382.
PubMed=25500261; DOI=10.1016/j.ajhg.2014.11.006;
Shinwari J.M., Khan A., Awad S., Shinwari Z., Alaiya A., Alanazi M.,
Tahir A., Poizat C., Al Tassan N.;
"Recessive mutations in COL25A1 are a cause of congenital cranial
dysinnervation disorder.";
Am. J. Hum. Genet. 96:147-152(2015).
-!- FUNCTION: Inhibits fibrillization of amyloid-beta peptide during
the elongation phase. Has also been shown to assemble amyloid
fibrils into protease-resistant aggregates. Binds heparin.
{ECO:0000269|PubMed:15522881, ECO:0000269|PubMed:15615705,
ECO:0000269|PubMed:15853808, ECO:0000269|PubMed:16300410}.
-!- SUBUNIT: Forms homodimers and homotrimers. Binds to the
fibrillized forms of amyloid-beta protein 40 (beta-APP40) and
amyloid-beta protein 42 (beta-APP42). Found associated with beta-
APP42 more frequently than with beta-APP40.
{ECO:0000269|PubMed:11927537, ECO:0000269|PubMed:15215182,
ECO:0000269|PubMed:15522881, ECO:0000269|PubMed:15615705}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
membrane protein {ECO:0000305}. Note=After proteolytic cleavage,
CLAC is secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1 {ECO:0000269|PubMed:11927537};
IsoId=Q9BXS0-1; Sequence=Displayed;
Name=2 {ECO:0000269|PubMed:11927537};
IsoId=Q9BXS0-2; Sequence=VSP_052200;
Name=3 {ECO:0000269|PubMed:14656069};
IsoId=Q9BXS0-3; Sequence=VSP_052197, VSP_052198, VSP_052199;
-!- TISSUE SPECIFICITY: Expressed predominantly in brain. Deposited
preferentially in primitive or neuritic amyloid plaques which are
typical of Alzheimer disease. {ECO:0000269|PubMed:11927537}.
-!- PTM: Undergoes proteolytic cleavage by furin protease to yield the
soluble collagen-like Alzheimer amyloid plaque component.
{ECO:0000269|PubMed:11927537}.
-!- PTM: Glycosylated. {ECO:0000269|PubMed:15522881}.
-!- PTM: Hydroxylated on 11% of proline residues and 49% of lysine
residues. {ECO:0000269|PubMed:11927537,
ECO:0000269|PubMed:15522881}.
-!- DISEASE: Fibrosis of extraocular muscles, congenital, 5 (CFEOM5)
[MIM:616219]: An ocular motility disorder characterized by
congenital dysinnervation of various cranial nerves to ocular
muscles. Clinical features are ophthalmoplegia, anchoring of the
eyes in downward gaze, ptosis, and backward tilt of the head.
{ECO:0000269|PubMed:25500261}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- CAUTION: The pyrrolidone carboxylic acid reported in
PubMed:11927537 probably formed artifactually from Glu-113 during
the extraction procedure in 70% formic acid. In PubMed:15522881,
the protein was found to have unblocked Glu at the N-terminus.
{ECO:0000305}.
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EMBL; AF293340; AAK35008.1; -; mRNA.
EMBL; AF293341; AAK35009.1; -; mRNA.
EMBL; AC097473; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC073427; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC095066; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC004701; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC004051; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS43258.1; -. [Q9BXS0-1]
CCDS; CCDS43259.1; -. [Q9BXS0-2]
RefSeq; NP_115907.2; NM_032518.2. [Q9BXS0-2]
RefSeq; NP_942014.1; NM_198721.3. [Q9BXS0-1]
UniGene; Hs.658842; -.
ProteinModelPortal; Q9BXS0; -.
BioGrid; 124143; 3.
ComplexPortal; CPX-1766; Collagen type XXV trimer, variant 1. [Q9BXS0-1]
ComplexPortal; CPX-390; Collagen type XXV trimer, variant 2. [Q9BXS0-2]
ComplexPortal; CPX-391; Collagen type XXV trimer, variant 3. [Q9BXS0-3]
STRING; 9606.ENSP00000382083; -.
iPTMnet; Q9BXS0; -.
PhosphoSitePlus; Q9BXS0; -.
BioMuta; COL25A1; -.
DMDM; 296434459; -.
EPD; Q9BXS0; -.
MaxQB; Q9BXS0; -.
PaxDb; Q9BXS0; -.
PeptideAtlas; Q9BXS0; -.
PRIDE; Q9BXS0; -.
ProteomicsDB; 79487; -.
ProteomicsDB; 79488; -. [Q9BXS0-2]
ProteomicsDB; 79489; -. [Q9BXS0-3]
Ensembl; ENST00000399126; ENSP00000382077; ENSG00000188517. [Q9BXS0-2]
Ensembl; ENST00000399132; ENSP00000382083; ENSG00000188517. [Q9BXS0-1]
GeneID; 84570; -.
KEGG; hsa:84570; -.
UCSC; uc062yyf.1; human. [Q9BXS0-1]
CTD; 84570; -.
DisGeNET; 84570; -.
EuPathDB; HostDB:ENSG00000188517.14; -.
GeneCards; COL25A1; -.
H-InvDB; HIX0004434; -.
HGNC; HGNC:18603; COL25A1.
HPA; HPA029107; -.
MalaCards; COL25A1; -.
MIM; 610004; gene.
MIM; 616219; phenotype.
neXtProt; NX_Q9BXS0; -.
OpenTargets; ENSG00000188517; -.
PharmGKB; PA134912284; -.
eggNOG; KOG3544; Eukaryota.
eggNOG; ENOG410ZYTY; LUCA.
GeneTree; ENSGT00900000140850; -.
HOGENOM; HOG000085653; -.
HOVERGEN; HBG101380; -.
InParanoid; Q9BXS0; -.
OrthoDB; EOG091G0G3Y; -.
PhylomeDB; Q9BXS0; -.
TreeFam; TF338175; -.
Reactome; R-HSA-1442490; Collagen degradation.
Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
Reactome; R-HSA-8948216; Collagen chain trimerization.
ChiTaRS; COL25A1; human.
GeneWiki; Collagen,_type_XXV,_alpha_1; -.
GenomeRNAi; 84570; -.
PRO; PR:Q9BXS0; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000188517; -.
CleanEx; HS_COL25A1; -.
ExpressionAtlas; Q9BXS0; baseline and differential.
Genevisible; Q9BXS0; HS.
GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005576; C:extracellular region; IDA:MGI.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0001540; F:amyloid-beta binding; IDA:UniProtKB.
GO; GO:0008201; F:heparin binding; IDA:UniProtKB.
GO; GO:0060385; P:axonogenesis involved in innervation; IEA:Ensembl.
InterPro; IPR008160; Collagen.
Pfam; PF01391; Collagen; 5.
1: Evidence at protein level;
Alternative splicing; Amyloid; Collagen; Complete proteome;
Direct protein sequencing; Disease mutation; Glycoprotein;
Heparin-binding; Hydroxylation; Membrane; Pyrrolidone carboxylic acid;
Reference proteome; Repeat; Signal-anchor; Transmembrane;
Transmembrane helix.
CHAIN 1 654 Collagen alpha-1(XXV) chain.
/FTId=PRO_0000259611.
CHAIN 113 654 Collagen-like Alzheimer amyloid plaque
component. {ECO:0000269|PubMed:11927537,
ECO:0000269|PubMed:15522881}.
/FTId=PRO_0000259612.
TOPO_DOM 1 33 Cytoplasmic. {ECO:0000255}.
TRANSMEM 34 54 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 55 654 Extracellular. {ECO:0000255}.
DOMAIN 121 164 Collagen-like 1. {ECO:0000255}.
DOMAIN 192 247 Collagen-like 2. {ECO:0000255}.
DOMAIN 249 308 Collagen-like 3. {ECO:0000255}.
DOMAIN 311 370 Collagen-like 4. {ECO:0000255}.
DOMAIN 372 425 Collagen-like 5. {ECO:0000255}.
DOMAIN 447 505 Collagen-like 6. {ECO:0000255}.
DOMAIN 571 630 Collagen-like 7. {ECO:0000255}.
REGION 181 188 Interaction with amyloid-beta peptide.
{ECO:0000269|PubMed:15522881}.
SITE 112 113 Cleavage; by furin.
MOD_RES 113 113 Pyrrolidone carboxylic acid (Glu).
{ECO:0000269|PubMed:11927537}.
VAR_SEQ 141 146 Missing (in isoform 3).
{ECO:0000303|PubMed:14656069}.
/FTId=VSP_052197.
VAR_SEQ 326 340 Missing (in isoform 3).
{ECO:0000303|PubMed:14656069}.
/FTId=VSP_052198.
VAR_SEQ 589 640 Missing (in isoform 3).
{ECO:0000303|PubMed:14656069}.
/FTId=VSP_052199.
VAR_SEQ 616 654 GFRGVKGEKGEPGQPGLDGLDAPCQLGPDGLPMPGCWQK
-> VTSPSQHVPCLILLLLSALLFSLCDSI (in
isoform 2).
{ECO:0000303|PubMed:11927537}.
/FTId=VSP_052200.
VARIANT 382 382 G -> R (in CFEOM5; causes loss of
stability; causes incorrect folding;
dbSNP:rs780209390).
{ECO:0000269|PubMed:25500261}.
/FTId=VAR_073325.
MUTAGEN 109 109 R->A: Not secreted.
{ECO:0000269|PubMed:11927537}.
MUTAGEN 112 112 R->A: Not secreted.
{ECO:0000269|PubMed:11927537}.
MUTAGEN 181 188 LIKRRLIK->VIKRRTFQ: Reduces binding to
amyloid-beta peptide.
{ECO:0000269|PubMed:15522881}.
MUTAGEN 181 188 Missing: Abolishes binding to amyloid-
beta peptide.
{ECO:0000269|PubMed:15522881}.
CONFLICT 28 28 A -> S (in Ref. 1; AAK35008 and 2;
AAK35009). {ECO:0000305}.
CONFLICT 427 427 E -> K (in Ref. 1; AAK35008 and 2;
AAK35009). {ECO:0000305}.
SEQUENCE 654 AA; 64771 MW; D6DFB4FB157C05A2 CRC64;
MLLKKHAGKG GGREPRSEDP TPAEQHCART MPPCAVLAAL LSVVAVVSCL YLGVKTNDLQ
ARIAALESAK GAPSIHLLPD TLDHLKTMVQ EKVERLLAQK SYEHMAKIRI AREAPSECNC
PAGPPGKRGK RGRRGESGPP GQPGPQGPPG PKGDKGEQGD QGPRMVFPKI NHGFLSADQQ
LIKRRLIKGD QGQAGPPGPP GPPGPRGPPG DTGKDGPRGM PGVPGEPGKP GEQGLMGPLG
PPGQKGSIGA PGIPGMNGQK GEPGLPGAVG QNGIPGPKGE PGEQGEKGDA GENGPKGDTG
EKGDPGSSAA GIKGEPGESG RPGQKGEPGL PGLPGLPGIK GEPGFIGPQG EPGLPGLPGT
KGERGEAGPP GRGERGEPGA PGPKGKQGES GTRGPKGSKG DRGEKGDSGA QGPRGPPGQK
GDQGATEIID YNGNLHEALQ RITTLTVTGP PGPPGPQGLQ GPKGEQGSPG IPGMDGEQGL
KGSKGDMGDP GMTGEKGGIG LPGLPGANGM KGEKGDSGMP GPQGPSIIGP PGPPGPHGPP
GPMGPHGLPG PKGTDGPMGP HGPAGPKGER GEKGAMGEPG PRGPYGLPGK DGEPGLDGFP
GPRGEKGDLG EKGEKGFRGV KGEKGEPGQP GLDGLDAPCQ LGPDGLPMPG CWQK


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