ID COQA1_HUMAN Reviewed; 441 AA.
AC Q96A83; Q32M90;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 27-MAR-2024, entry version 157.
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=EMID2, EMU2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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. {ECO:0000250}.
CC -!- INTERACTION:
CC Q96A83-2; Q9NP70: AMBN; NbExp=3; IntAct=EBI-21553822, EBI-11893530;
CC Q96A83-2; P13928: ANXA8; NbExp=3; IntAct=EBI-21553822, EBI-2556915;
CC Q96A83-2; P05067: APP; NbExp=3; IntAct=EBI-21553822, EBI-77613;
CC Q96A83-2; Q8TBE0: BAHD1; NbExp=3; IntAct=EBI-21553822, EBI-742750;
CC Q96A83-2; Q14457: BECN1; NbExp=3; IntAct=EBI-21553822, EBI-949378;
CC Q96A83-2; Q96SW2: CRBN; NbExp=3; IntAct=EBI-21553822, EBI-2510250;
CC Q96A83-2; Q86TI2-2: DPP9; NbExp=3; IntAct=EBI-21553822, EBI-21529239;
CC Q96A83-2; Q9H410: DSN1; NbExp=3; IntAct=EBI-21553822, EBI-1001144;
CC Q96A83-2; Q8WVX9: FAR1; NbExp=3; IntAct=EBI-21553822, EBI-1045879;
CC Q96A83-2; Q5TD97: FHL5; NbExp=3; IntAct=EBI-21553822, EBI-750641;
CC Q96A83-2; Q06547-3: GABPB1; NbExp=3; IntAct=EBI-21553822, EBI-9088619;
CC Q96A83-2; Q6NXT2: H3-5; NbExp=3; IntAct=EBI-21553822, EBI-2868501;
CC Q96A83-2; Q14005-2: IL16; NbExp=3; IntAct=EBI-21553822, EBI-17178971;
CC Q96A83-2; Q0VD86: INCA1; NbExp=3; IntAct=EBI-21553822, EBI-6509505;
CC Q96A83-2; Q8NA54: IQUB; NbExp=3; IntAct=EBI-21553822, EBI-10220600;
CC Q96A83-2; Q9UIH9: KLF15; NbExp=3; IntAct=EBI-21553822, EBI-2796400;
CC Q96A83-2; Q13887: KLF5; NbExp=3; IntAct=EBI-21553822, EBI-2696013;
CC Q96A83-2; Q9BV99: LRRC61; NbExp=3; IntAct=EBI-21553822, EBI-2350424;
CC Q96A83-2; P02795: MT2A; NbExp=3; IntAct=EBI-21553822, EBI-996616;
CC Q96A83-2; P22061-2: PCMT1; NbExp=3; IntAct=EBI-21553822, EBI-12386584;
CC Q96A83-2; Q8IXK0-5: PHC2; NbExp=3; IntAct=EBI-21553822, EBI-11527347;
CC Q96A83-2; Q8IUQ4-2: SIAH1; NbExp=3; IntAct=EBI-21553822, EBI-11522811;
CC Q96A83-2; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-21553822, EBI-358489;
CC Q96A83-2; O75886: STAM2; NbExp=3; IntAct=EBI-21553822, EBI-373258;
CC Q96A83-2; O75558: STX11; NbExp=3; IntAct=EBI-21553822, EBI-714135;
CC Q96A83-2; Q86WV8: TSC1; NbExp=3; IntAct=EBI-21553822, EBI-12806590;
CC Q96A83-2; Q6PF05: TTC23L; NbExp=3; IntAct=EBI-21553822, EBI-8656864;
CC Q96A83-2; Q6PID6: TTC33; NbExp=3; IntAct=EBI-21553822, EBI-2555404;
CC Q96A83-2; Q9BRX9: WDR83; NbExp=3; IntAct=EBI-21553822, EBI-7705033;
CC Q96A83-2; Q9H4I2-2: ZHX3; NbExp=3; IntAct=EBI-21553822, EBI-10693326;
CC Q96A83-2; Q96MN9-2: ZNF488; NbExp=3; IntAct=EBI-21553822, EBI-25831733;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96A83-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96A83-2; Sequence=VSP_008447;
CC -!- PTM: Hydroxylated on proline residues. {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
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DR EMBL; AJ416091; CAC94778.1; -; mRNA.
DR EMBL; AC004953; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC004965; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC006329; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC109254; AAI09255.1; -; mRNA.
DR EMBL; BC110393; AAI10394.1; -; mRNA.
DR CCDS; CCDS64739.1; -. [Q96A83-1]
DR RefSeq; NP_001265492.1; NM_001278563.2. [Q96A83-1]
DR RefSeq; NP_597714.2; NM_133457.4. [Q96A83-2]
DR PDB; 4AU2; X-ray; 2.30 A; E/F/G/H/I/J=312-325.
DR PDB; 4AU3; X-ray; 2.78 A; E/F/G/H/I/J=309-326.
DR PDB; 4BJ3; X-ray; 3.04 A; C/D/E=308-326.
DR PDB; 7BDU; X-ray; 2.49 A; C/D/E/F/G/H=309-329.
DR PDB; 7BEE; X-ray; 1.94 A; C/D/E/F/G/H=309-329.
DR PDB; 7BFI; X-ray; 2.44 A; E/F/G/H/I/J=312-326.
DR PDBsum; 4AU2; -.
DR PDBsum; 4AU3; -.
DR PDBsum; 4BJ3; -.
DR PDBsum; 7BDU; -.
DR PDBsum; 7BEE; -.
DR PDBsum; 7BFI; -.
DR AlphaFoldDB; Q96A83; -.
DR SMR; Q96A83; -.
DR BioGRID; 126448; 4.
DR ComplexPortal; CPX-1767; Collagen type XXVI trimer.
DR IntAct; Q96A83; 34.
DR STRING; 9606.ENSP00000318234; -.
DR GlyCosmos; Q96A83; 3 sites, 3 glycans.
DR GlyGen; Q96A83; 7 sites, 4 O-linked glycans (5 sites).
DR iPTMnet; Q96A83; -.
DR PhosphoSitePlus; Q96A83; -.
DR BioMuta; COL26A1; -.
DR DMDM; 37537825; -.
DR EPD; Q96A83; -.
DR jPOST; Q96A83; -.
DR MassIVE; Q96A83; -.
DR PaxDb; 9606-ENSP00000318234; -.
DR PeptideAtlas; Q96A83; -.
DR ProteomicsDB; 75933; -. [Q96A83-1]
DR ProteomicsDB; 75934; -. [Q96A83-2]
DR Antibodypedia; 9137; 185 antibodies from 24 providers.
DR DNASU; 136227; -.
DR Ensembl; ENST00000313669.12; ENSP00000318234.8; ENSG00000160963.14. [Q96A83-1]
DR Ensembl; ENST00000613501.1; ENSP00000482102.1; ENSG00000160963.14. [Q96A83-2]
DR GeneID; 136227; -.
DR KEGG; hsa:136227; -.
DR MANE-Select; ENST00000313669.12; ENSP00000318234.8; NM_001278563.3; NP_001265492.1.
DR UCSC; uc033aas.1; human. [Q96A83-1]
DR AGR; HGNC:18038; -.
DR CTD; 136227; -.
DR DisGeNET; 136227; -.
DR GeneCards; COL26A1; -.
DR HGNC; HGNC:18038; COL26A1.
DR HPA; ENSG00000160963; Tissue enriched (brain).
DR MIM; 608927; gene.
DR neXtProt; NX_Q96A83; -.
DR OpenTargets; ENSG00000160963; -.
DR PharmGKB; PA134887081; -.
DR VEuPathDB; HostDB:ENSG00000160963; -.
DR eggNOG; ENOG502R2C0; Eukaryota.
DR GeneTree; ENSGT00940000161716; -.
DR HOGENOM; CLU_045268_1_0_1; -.
DR InParanoid; Q96A83; -.
DR OMA; TCKVHNG; -.
DR OrthoDB; 3062338at2759; -.
DR PhylomeDB; Q96A83; -.
DR PathwayCommons; Q96A83; -.
DR Reactome; R-HSA-1442490; Collagen degradation.
DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-HSA-8948216; Collagen chain trimerization.
DR SignaLink; Q96A83; -.
DR BioGRID-ORCS; 136227; 4 hits in 603 CRISPR screens.
DR ChiTaRS; COL26A1; human.
DR GeneWiki; EMID2; -.
DR GenomeRNAi; 136227; -.
DR Pharos; Q96A83; Tbio.
DR PRO; PR:Q96A83; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q96A83; Protein.
DR Bgee; ENSG00000160963; Expressed in vena cava and 143 other cell types or tissues.
DR Genevisible; Q96A83; HS.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:Ensembl.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR011489; EMI_domain.
DR PANTHER; PTHR15427:SF19; COLLAGEN ALPHA-1(XXVI) CHAIN; 1.
DR PANTHER; PTHR15427; EMILIN ELASTIN MICROFIBRIL INTERFACE-LOCATED PROTEIN ELASTIN MICROFIBRIL INTERFACER; 1.
DR Pfam; PF01391; Collagen; 2.
DR Pfam; PF07546; EMI; 1.
DR PROSITE; PS51041; EMI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Collagen; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Hydroxylation; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..441
FT /note="Collagen alpha-1(XXVI) chain"
FT /id="PRO_0000007825"
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..355
FT /note="Collagen-like 2"
FT REGION 156..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..441
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..267
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..286
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 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:12221002,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_008447"
FT VARIANT 427
FT /note="P -> L (in dbSNP:rs17471501)"
FT /id="VAR_057530"
SQ SEQUENCE 441 AA; 45381 MW; 896CA2AC52B20E92 CRC64;
MKLALLLPWA CCCLCGSALA TGFLYPFSAA ALQQHGYPEP GAGSPGSGYA SRRHWCHHTV
TRTVSCQVQN GSETVVQRVY QSCRWPGPCA NLVSYRTLIR PTYRVSYRTV TVLEWRCCPG
FTGSNCDEEC MNCTRLSDMS ERLTTLEAKV LLLEAAERPS SPDNDLPAPE STPPTWNEDF
LPDAIPLAHP VPRQRRPTGP AGPPGQTGPP GPAGPPGSKG DRGQTGEKGP AGPPGLLGPP
GPRGLPGEMG RPGPPGPPGP AGNPGPSPNS PQGALYSLQP PTDKDNGDSR LASAIVDTVL
AGVPGPRGPP GPPGPPGPRG PPGPPGTPGS QGLAGERGTV GPSGEPGVKG EEGEKAATAE
GEGVQQLREA LKILAERVLI LEHMIGIHDP LASPEGGSGQ DAALRANLKM KRGGAQPDGV
LAALLGPDPG QKSVDQASSR K
//
