ID A0A674GP97_TAEGU Unreviewed; 1685 AA.
AC A0A674GP97;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 23.
DE SubName: Full=Collagen type XVIII alpha 1 chain {ECO:0000313|Ensembl:ENSTGUP00000024291.1};
GN Name=COL18A1 {ECO:0000313|Ensembl:ENSTGUP00000024291.1};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Passeroidea; Estrildidae; Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000024291.1, ECO:0000313|Proteomes:UP000007754};
RN [1] {ECO:0000313|Ensembl:ENSTGUP00000024291.1, ECO:0000313|Proteomes:UP000007754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20360741; DOI=10.1038/nature08819;
RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT "The genome of a songbird.";
RL Nature 464:757-762(2010).
RN [2] {ECO:0000313|Ensembl:ENSTGUP00000024291.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSTGUP00000024291.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- SIMILARITY: Belongs to the multiplexin collagen family.
CC {ECO:0000256|ARBA:ARBA00061275}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR Ensembl; ENSTGUT00000039837.1; ENSTGUP00000024291.1; ENSTGUG00000003295.2.
DR CTD; 80781; -.
DR GeneTree; ENSGT00940000158212; -.
DR InParanoid; A0A674GP97; -.
DR Proteomes; UP000007754; Chromosome 7.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; IEA:TreeGrafter.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR CDD; cd00247; Endostatin-like; 1.
DR FunFam; 3.10.100.10:FF:000008; collagen alpha-1(XVIII) chain isoform X1; 1.
DR FunFam; 2.60.120.200:FF:000039; Collagen XV alpha 1 chain; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.40.1620.70; -; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR050149; Collagen_superfamily.
DR InterPro; IPR010515; Collagenase_NC10/endostatin.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR Pfam; PF01391; Collagen; 5.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000007754};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1685
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025327953"
FT DOMAIN 381..569
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 39..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..1117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1129..1368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..60
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..585
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..632
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..667
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..760
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..803
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..843
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..883
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..935
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..955
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..991
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1044
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1185..1198
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1202..1213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1254..1268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1273..1282
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1305..1314
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1325..1338
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1348..1360
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1685 AA; 173136 MW; 6BBE77090ECDAFEB CRC64;
MAPSCLGFLL FLACCFSCSE TQLLDWVWDS TKTAGSPAVL GEGIPASEPP TSATAPSPSS
GMWGGEVAGN VTTPWQQEPD PATAAPVGKG TAAKTTEQWD RNGTGLVEST AWPSIAPLHS
MSPAPGQLAA STDDSQLLGS GTTEDLQLPG SETSKDPQVL WSGNTEDLQL LETGTTEHLL
LQRMRTTKDP QFLGSVTPKD PQLLETGTAE DLKLLGSGTT ENPQLLGMGT TEDPQLLGSG
TTEDLQLLGL GATEDPQLLG MMSTTDLQLL VTGRTKDPQL LGAGTTEDPQ FLGAGTTEDP
QLPGMRTTGN LQLLAMRNTQ FLRTVTTENP ELLGNTENPQ FLRTITTKNP EFLGTGTSTA
METQVSLQRP AGLQPESLSA EISLLELIGD PPTEEIHRIY GPDNNPGYVF GPNANTGQVA
RYHLPSPFYR DFSLLFHIQP TTPRAGVLFA VTDASQSIIY VGVKLSELRA GQQQIIFYYT
EPGSPSSYPA ATFTVPTLLN QWTRFAISVE EEEVVLYLDC EEHERVRFER SPDEMELEEG
SGLFVAQAGG ADPDKYQGVI ADLKLRGDPR AAERQCEEEE DDAEVSGDFG SGMEGGQQSL
SKAEGVPGLV DAVPVTSPPV VGGSGPRSGG GSLQQAERTR AEETLRVPTG GTGQKGEKGE
KGERGLKGDS GTSGIVGPGS VKGQKGEKGD LGVKGSAGFG YPGSKGQKGE PGNPGPPGTL
SRHADGSVVE QVTGPPGTPG KDGAPGRDGE PGDPGEDGKP GEMGPPGFPG MPGEPGLKGE
KGDPGMGPRG PPGPPGPPGP PGPSSKNDKL TFIDMEGSGF GGDLESLRGP RGPPGPPGPP
GVPGLPGEPG RFGMNCTDLP GPPGLPGRDG IPGPPGPVGP QGPPGRDGEV GQPGPKGEQG
DVGDLGLPGL PGPKGNKGEM GPAGPPGEMG LAGLPGPIGP RGQPGPPGPP GPPGPGYEAG
FGDMEGSGLS FTPGPPGPEG PQGVPGLPGV KGEVGSPGQP GLPGPKGDAG MPGMDGRPGP
EGFPGPQGPK GDKGSTGEKG ERGQDGVGLP GPPGPPGQVI SVSSEDKSLV AFPGPEGRPG
RAGFPGPVGP KGDQGSTGPQ GAPGLKGEKG EPGVIISPDG TVVTAKVKGE KGEPGLQGPT
GPSGPPGRAG MKGEIGFPGR PGRPGMNGLK GEKGDPADVL GLRGPPGPPG PPGPPGPPGS
IVYNNGNTFS DSSHPAFRGF HQFSGQKGEK GDTGPPGPPG QFPYDASHFG TSLRGDKGDA
GPKGEKGEPG STPLYGPGVS GLPGPPGPQG YPGLPGPKGD SIVGPPGPPG PQGPPGIGYE
GRQGPPGPPG PPGPPSFPGP HRQAVSIPGP PGPPGPPGPP GSSGMSLGLQ AMPTYQAMLS
AAHELPEGSL VFLRDREELH VRLRGGFRRV LLEEHNLIPS SALDNEVYDK PPTLHYAGPQ
PRGPLHPLRN HVPSATARPW HGDEVVANQH RLPEQPLLHH QHELINGYYI HRRPDPAPVA
AHVHQDFQPA LHLVALNTPL SGGMRGIRGA DFQCFQQARQ VGLAGTFRAF LSSRLQDLYS
IVRRADRAAV PIVNLRDEVL FSNWEALFTG SGAPLRTGAR ILSFDGRDVL RDAGWPQKSV
WHGSDAKGRR LPESYCETWR TEERAVVGQA SSLASGKLLE QAASSCQHAF IVLCIENSFM
TATKK
//
