COSA1_MOUSE
ID COSA1_MOUSE Reviewed; 1141 AA.
AC Q2UY11; Q2UY10;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Collagen alpha-1(XXVIII) chain;
DE Flags: Precursor;
GN Name=Col28a1; Synonyms=Col28;
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] (ISOFORMS 1 AND 2), SUBUNITS, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Limb;
RX PubMed=16330543; DOI=10.1074/jbc.m509333200;
RA Veit G., Kobbe B., Keene D.R., Paulsson M., Koch M., Wagener R.;
RT "Collagen XXVIII, a novel von Willebrand factor A domain-containing protein
RT with many imperfections in the collagenous domain.";
RL J. Biol. Chem. 281:3494-3504(2006).
CC -!- FUNCTION: May act as a cell-binding protein.
CC -!- SUBUNIT: Trimer or homomer. Secreted into as a 135 kDa monomer under
CC reducing conditions and as a homotrimer under non-reducing conditions.
CC {ECO:0000269|PubMed:16330543}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000269|PubMed:16330543}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q2UY11-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2UY11-2; Sequence=VSP_031095, VSP_031096;
CC -!- TISSUE SPECIFICITY: Expressed in skin, intestine, sternum, brain and
CC kidney. Lower expression is also observed in heart, lung, sciatic
CC nerve, dorsal root ganglia, peripheral nerves and calvaria of newborn
CC mice and in intestine and brain of adult mice. Found in basement
CC membrane surrounding a particular subset of Schwann cells in adult
CC sciatic nerve. {ECO:0000269|PubMed:16330543}.
CC -!- DEVELOPMENTAL STAGE: Major expression in dorsal root ganglia and
CC peripheral nerves, with small amounts in connective tissues like
CC calvaria and skin. {ECO:0000269|PubMed:16330543}.
CC -!- SIMILARITY: Belongs to the VWA-containing collagen family.
CC {ECO:0000305}.
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DR EMBL; AJ890449; CAI67593.1; -; mRNA.
DR EMBL; AJ890450; CAI67594.1; -; mRNA.
DR CCDS; CCDS39424.1; -. [Q2UY11-1]
DR RefSeq; NP_001032954.1; NM_001037865.1. [Q2UY11-1]
DR RefSeq; XP_006505094.1; XM_006505031.2. [Q2UY11-1]
DR RefSeq; XP_006505095.1; XM_006505032.3. [Q2UY11-1]
DR RefSeq; XP_017176991.1; XM_017321502.1. [Q2UY11-1]
DR AlphaFoldDB; Q2UY11; -.
DR SMR; Q2UY11; -.
DR ComplexPortal; CPX-3029; Collagen type XXVIII trimer.
DR STRING; 10090.ENSMUSP00000111199; -.
DR PhosphoSitePlus; Q2UY11; -.
DR MaxQB; Q2UY11; -.
DR PaxDb; Q2UY11; -.
DR PRIDE; Q2UY11; -.
DR ProteomicsDB; 277995; -. [Q2UY11-1]
DR ProteomicsDB; 277996; -. [Q2UY11-2]
DR Antibodypedia; 71450; 23 antibodies from 11 providers.
DR DNASU; 213945; -.
DR Ensembl; ENSMUST00000115537; ENSMUSP00000111199; ENSMUSG00000068794. [Q2UY11-1]
DR GeneID; 213945; -.
DR KEGG; mmu:213945; -.
DR UCSC; uc009axi.1; mouse. [Q2UY11-1]
DR CTD; 340267; -.
DR MGI; MGI:2685312; Col28a1.
DR VEuPathDB; HostDB:ENSMUSG00000068794; -.
DR eggNOG; KOG1217; Eukaryota.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000161647; -.
DR HOGENOM; CLU_009158_0_0_1; -.
DR InParanoid; Q2UY11; -.
DR OMA; VINYSHK; -.
DR OrthoDB; 293907at2759; -.
DR PhylomeDB; Q2UY11; -.
DR TreeFam; TF331207; -.
DR Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-MMU-8948216; Collagen chain trimerization.
DR BioGRID-ORCS; 213945; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Col28a1; mouse.
DR PRO; PR:Q2UY11; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q2UY11; protein.
DR Bgee; ENSMUSG00000068794; Expressed in spermatocyte and 38 other tissues.
DR ExpressionAtlas; Q2UY11; baseline and differential.
DR GO; GO:0005604; C:basement membrane; IDA:MGI.
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:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR CDD; cd00109; KU; 1.
DR Gene3D; 3.40.50.410; -; 2.
DR Gene3D; 4.10.410.10; -; 1.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF01391; Collagen; 1.
DR Pfam; PF00014; Kunitz_BPTI; 1.
DR Pfam; PF00092; VWA; 2.
DR SMART; SM00131; KU; 1.
DR SMART; SM00327; VWA; 2.
DR SUPFAM; SSF53300; SSF53300; 2.
DR SUPFAM; SSF57362; SSF57362; 1.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 1.
DR PROSITE; PS50234; VWFA; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Basement membrane; Cell adhesion; Collagen;
KW Disulfide bond; Extracellular matrix; Protease inhibitor;
KW Reference proteome; Repeat; Secreted; Serine protease inhibitor; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1141
FT /note="Collagen alpha-1(XXVIII) chain"
FT /id="PRO_5000074665"
FT DOMAIN 48..227
FT /note="VWFA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 243..300
FT /note="Collagen-like 1"
FT DOMAIN 301..358
FT /note="Collagen-like 2"
FT DOMAIN 501..544
FT /note="Collagen-like 3"
FT DOMAIN 545..588
FT /note="Collagen-like 4"
FT DOMAIN 733..769
FT /note="Collagen-like 5"
FT DOMAIN 798..976
FT /note="VWFA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 1088..1138
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT REGION 242..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..754
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1088..1138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 1097..1121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 1113..1134
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT VAR_SEQ 667..699
FT /note="GEPGVRGPPGPSGPRGIGTQGPKGDTGQKGLPG -> VRFLKEAKILVFKKV
FT LIDDFGKCVLFLSGTQEE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16330543"
FT /id="VSP_031095"
FT VAR_SEQ 700..1141
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16330543"
FT /id="VSP_031096"
SQ SEQUENCE 1141 AA; 118749 MW; A2C43C4BB7913272 CRC64;
MRRRDVAFCL LLLPAFMTQA VYGQRKKGPK PNTLARKNDF QDAICFIDVV FILDSSESSK
IVLFDNQKDF VDSLSEKIFQ LTPGRSLKYD IKLAALQFSS SVQIDPPLSS WKDLRTFKQR
VKSLNLIGQG TFSYYAISNA TRLLKREGRK DGVKVALLMT DGIDHPKSPD VQSISEDARI
LGISFITVGL STVVNEAKLR LISGDPSNEP VLLLSDPTLV DRIQERLGVL FERKCEHKIC
ECEKGEPGDP GPPGTHGNPG IKGERGPKGN PGDAQKGETG ERGPVGIPGY KGDKGERGEC
GKPGMKGDKG PEGPYGPKGP RGIQGIGGPP GDPGPKGFQG NKGEPGPPGP YGPPGAPGIG
QQGVKGERGQ EGRMGAPGPI GIGEPGQPGP RGPEGAPGER GLPGEGFPGP KGEKGSEGPI
GPQGLQGLSI KGDKGDLGPV GPQGPAGIPG IGSQGEQGIQ GPSGPPGPQG PPGQGSPGPK
GEVGQMGPTG PRGPMGIGVQ GPKGEPGTVG LPGQPGVPGE DGASGKKGEA GLPGTRGPEG
MPGKGQPGPK GDEGKKGSKG NQGQRGFPGP EGPKGEPGVM GPFGMPGASI PGPSGPKGDR
GGPGMPGLKG EPGLPVRGPK GAQGPRGPVG APGLKGDGYP GVAGPRGLPG PPGPMGLRGV
GDTGAKGEPG VRGPPGPSGP RGIGTQGPKG DTGQKGLPGP PGPPGYGSQG IKGEQGPQGF
PGSKGTVGLG LPGQKGEHGD RGDVGRKGEK GETGEPGSPG KQGLQGPKGD LGLTKEEIIK
LIIEICGCGP KCKETPLELV FVIDSSESVG PENFQIIQSF VKTLADRVAL DLGTARIGII
NYSHKVEKVA SLKQFSSKDD FKLVVDNMQY LGEGTYTATA LQAANDMFKE ARPGVKKVAL
VITDGQTDSR DKKKLADVVK DANDSNVEIF VIGVVKKDDP NFEIFHKEMN LIATDAEHVY
QFDDFFTLQD TLKQKLSKKI CEDFDSYLIQ VFGSPSFQPE FGVSEREVSV STPKPAKEMS
KSFNVSRGQN EETESYVLTE AGILAIPTPP EATNTLEPLL SSREGVETRT PNPNLLQSEK
SLYKDPRCEE ALKPGECGDY VVRWYYDKQV NSCARFWFSG CNGSGNRFHS EKECRETCIK
Q
