ID A0A674H3F2_TAEGU Unreviewed; 1312 AA.
AC A0A674H3F2;
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:ENSTGUP00000029976.1};
GN Name=COL18A1 {ECO:0000313|Ensembl:ENSTGUP00000029976.1};
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:ENSTGUP00000029976.1, ECO:0000313|Proteomes:UP000007754};
RN [1] {ECO:0000313|Ensembl:ENSTGUP00000029976.1, 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:ENSTGUP00000029976.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSTGUP00000029976.1}
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}.
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DR Ensembl; ENSTGUT00000030205.1; ENSTGUP00000029976.1; ENSTGUG00000003295.2.
DR GeneTree; ENSGT00940000158212; -.
DR Proteomes; UP000007754; Chromosome 7.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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; IPR050938; Collagen_Structural_Proteins.
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; PTHR37456:SF6; COLLAGEN ALPHA-1(XXIII) CHAIN-LIKE ISOFORM X2; 1.
DR PANTHER; PTHR37456; SI:CH211-266K2.1; 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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1312
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025541721"
FT DOMAIN 32..220
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 219..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 756..995
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..236
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..283
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..454
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..494
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..534
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..586
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..606
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..671
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..825
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..840
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..895
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..909
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..941
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..965
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..987
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1312 AA; 134307 MW; 9460B712EA06CCF1 CRC64;
MRTGCPPPRL LLGFFVLLVP AASQEPESLS AEISLLELIG DPPTEEIHRI YGPDNNPGYV
FGPNANTGQV ARYHLPSPFY RDFSLLFHIQ PTTPRAGVLF AVTDASQSII YVGVKLSELR
AGQQQIIFYY TEPGSPSSYP AATFTVPTLL NQWTRFAISV EEEEVVLYLD CEEHERVRFE
RSPDEMELEE GSGLFVAQAG GADPDKYQGV IADLKLRGDP RAAERQCEEE EDDAEVSGDF
GSGMEGGQQS LSKAEGVPGL VDAVPVTSPP VVGGSGPRSG GGSLQQAERT RAEETLRVPT
GGTGQKGEKG EKGERGLKGD SGTSGIVGPG SVKGQKGEKG DLGVKGSAGF GYPGSKGQKG
EPGNPGPPGT LSRHADGSVV EQVTGPPGTP GKDGAPGRDG EPGDPGEDGK PGEMGPPGFP
GMPGEPGLKG EKGDPGMGPR GPPGPPGPPG PPGPSSKNDK LTFIDMEGSG FGGDLESLRG
PRGPPGPPGP PGVPGLPGEP GRFGMNCTDL PGPPGLPGRD GIPGPPGPVG PQGPPGRDGE
VGQPGPKGEQ GDVGDLGLPG LPGPKGNKGE MGPAGPPGEM GLAGLPGPIG PRGQPGPPGP
PGPPGPGYEA GFGDMEGSGL SFTPGPPGPE GPQGDAGMPG MDGRPGPEGF PGPQGPKGDK
GSTGEKGERG QDGVGLPGPP GPPGQVISVS SEDKSLVAFP GPEGRPGRAG FPGPVGPKGD
QGSTGPQGAP GLKGEKGEPG VIISPDGTVV TAKVKGEKGE PGLQGPTGPS GPPGRAGMKG
EIGFPGRPGR PGMNGLKGEK GDPADVLGLR GPPGPPGPPG PPGPPGSIVY NNGNTFSDSS
HPAFRGFHQF SGQKGEKGDT GPPGPPGQFP YDASHFGTSL RGDKGDAGPK GEKGEPGSTP
LYGPGVSGLP GPPGPQGYPG LPGPKGDSIV GPPGPPGPQG PPGIGYEGRQ GPPGPPGPPG
PPSFPGPHRQ AVSIPGPPGP PGPPGPPGSS GMSLGLQAMP TYQAMLSAAH ELPEGSLVFL
RDREELHVRL RGGFRRVLLE EHNLIPSSAL DNEVYDKPPT LHYAGPQPRG PLHPLRNHVP
SATARPWHGD EVVANQHRLP EQPLLHHQHE LINGYYIHRR PDPAPVAAHV HQDFQPALHL
VALNTPLSGG MRGIRGADFQ CFQQARQVGL AGTFRAFLSS RLQDLYSIVR RADRAAVPIV
NLRDEVLFSN WEALFTGSGA PLRTGARILS FDGRDVLRDA GWPQKSVWHG SDAKGRRLPE
SYCETWRTEE RAVVGQASSL ASGKLLEQAA SSCQHAFIVL CIENSFMTAT KK
//
