COQA1_MOUSE
ID COQA1_MOUSE Reviewed; 440 AA.
AC Q91VF6; Q8K4P3;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Collagen alpha-1(XXVI) chain;
DE AltName: Full=Alpha-1 type XXVI collagen;
DE AltName: Full=EMI domain-containing protein 2;
DE AltName: Full=Emilin and multimerin domain-containing protein 2;
DE Short=Emu2;
DE Flags: Precursor;
GN Name=Col26a1; Synonyms=Col26a, Emid2, Emu2;
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] (ISOFORM 2), CHARACTERIZATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=12145293; DOI=10.1074/jbc.m205347200;
RA Sato K., Yomogida K., Wada T., Yorihuzi T., Nishimune Y., Hosokawa N.,
RA Nagata K.;
RT "Type XXVI collagen, a new member of the collagen family, is specifically
RT expressed in the testis and ovary.";
RL J. Biol. Chem. 277:37678-37684(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX PubMed=12221002; DOI=10.1006/dbio.2002.0764;
RA Leimeister C., Steidl C., Schumacher N., Erhard S., Gessler M.;
RT "Developmental expression and biochemical characterization of Emu family
RT members.";
RL Dev. Biol. 249:204-218(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Olfactory epithelium;
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).
CC -!- SUBUNIT: Homotrimer or heterotrimer.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q91VF6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91VF6-2; Sequence=VSP_008448;
CC -!- TISSUE SPECIFICITY: Specifically expressed in the testis and ovary in
CC adult tissues. {ECO:0000269|PubMed:12145293}.
CC -!- DEVELOPMENTAL STAGE: At 9.5 dpc it is expressed in the somites and in
CC mesenchymal cells of the head and the branchial arches. At 14.5 dpc it
CC is expressed in the surrounding mesenchyme of the kidney and the inner
CC ear. Expression is also observed in the spinal nerves and ganglia, the
CC mesenchyme of the skull, the diaphragm, and the skeletal muscles.
CC -!- PTM: Hydroxylated on proline residues.
CC -!- PTM: N-glycosylated.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
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DR EMBL; AB085837; BAB96760.1; -; mRNA.
DR EMBL; AJ416092; CAC94779.1; -; mRNA.
DR EMBL; BC075713; AAH75713.1; -; mRNA.
DR CCDS; CCDS19755.1; -. [Q91VF6-1]
DR CCDS; CCDS84976.1; -. [Q91VF6-2]
DR RefSeq; NP_001333628.1; NM_001346699.1. [Q91VF6-2]
DR RefSeq; NP_077794.2; NM_024474.2. [Q91VF6-1]
DR AlphaFoldDB; Q91VF6; -.
DR BioGRID; 228305; 2.
DR ComplexPortal; CPX-3007; Collagen type XXVI trimer.
DR STRING; 10090.ENSMUSP00000052095; -.
DR GlyGen; Q91VF6; 2 sites.
DR iPTMnet; Q91VF6; -.
DR PhosphoSitePlus; Q91VF6; -.
DR MaxQB; Q91VF6; -.
DR PaxDb; Q91VF6; -.
DR PRIDE; Q91VF6; -.
DR ProteomicsDB; 277992; -. [Q91VF6-1]
DR ProteomicsDB; 277993; -. [Q91VF6-2]
DR Antibodypedia; 9137; 163 antibodies from 24 providers.
DR Ensembl; ENSMUST00000057497; ENSMUSP00000052095; ENSMUSG00000004415. [Q91VF6-1]
DR Ensembl; ENSMUST00000111103; ENSMUSP00000106732; ENSMUSG00000004415. [Q91VF6-2]
DR GeneID; 140709; -.
DR KEGG; mmu:140709; -.
DR UCSC; uc009aay.1; mouse. [Q91VF6-1]
DR UCSC; uc009aaz.1; mouse. [Q91VF6-2]
DR CTD; 136227; -.
DR MGI; MGI:2155345; Col26a1.
DR VEuPathDB; HostDB:ENSMUSG00000004415; -.
DR eggNOG; ENOG502R2C0; Eukaryota.
DR GeneTree; ENSGT00940000161716; -.
DR HOGENOM; CLU_045268_1_0_1; -.
DR InParanoid; Q91VF6; -.
DR OMA; GGRRHWC; -.
DR OrthoDB; 1205089at2759; -.
DR PhylomeDB; Q91VF6; -.
DR TreeFam; TF336589; -.
DR Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-MMU-8948216; Collagen chain trimerization.
DR BioGRID-ORCS; 140709; 0 hits in 76 CRISPR screens.
DR ChiTaRS; Col26a1; mouse.
DR PRO; PR:Q91VF6; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q91VF6; protein.
DR Bgee; ENSMUSG00000004415; Expressed in secondary palatal shelf and 139 other tissues.
DR Genevisible; Q91VF6; MM.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IDA:MGI.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR011489; EMI_domain.
DR Pfam; PF01391; Collagen; 2.
DR Pfam; PF07546; EMI; 1.
DR PROSITE; PS51041; EMI; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Collagen; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Hydroxylation; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..440
FT /note="Collagen alpha-1(XXVI) chain"
FT /id="PRO_0000007826"
FT DOMAIN 52..128
FT /note="EMI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DOMAIN 199..267
FT /note="Collagen-like 1"
FT DOMAIN 302..334
FT /note="Collagen-like 2"
FT REGION 157..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..216
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..265
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..328
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..358
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 56..118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DISULFID 83..89
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DISULFID 117..126
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT VAR_SEQ 94..95
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12145293,
FT ECO:0000303|PubMed:12221002"
FT /id="VSP_008448"
SQ SEQUENCE 440 AA; 45810 MW; 10843475F53A2BB0 CRC64;
MKLVLLLPWA CCCLCGSALA TGFLYPFPAA ALQQHGYPEQ GAGSPGNGYS SRRHWCHHTV
TRTVSCQVQN GSETVVQRVY QSCRWPGPCA NLVSYRTLIR PTYRVSYRTV TALEWRCCPG
FTGSNCEEEC MNCTRLSDMS ERLTTLEAKV LLLEAAEQPS GPDNDLPPPQ STPPTWNEDF
LPDAIPIAHP GPRRRRPTGP AGPPGQMGPP GPAGPPGSKG EQGQTGEKGP VGPPGLLGPP
GPRGLPGEMG RPGPPGPPGP AGSPGLLPNT PQGVLYSLQT PTDKENGDSQ LNPAVVDTVL
TGIPGPRGPP GPPGPPGPHG PPGPPGAPGS QGLVDERVVA RPSGEPSVKE EEDKASAAEG
EGVQQLREAL KILAERVLIL EHMIGVHDPL ASPEGGSGQD AALRANLKMK RGGPRPDGIL
AALLGPDPAQ KSADQAGDRK
