ID A0A8C4U0X7_FALTI Unreviewed; 1352 AA.
AC A0A8C4U0X7;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE SubName: Full=Collagen type XVIII alpha 1 chain {ECO:0000313|Ensembl:ENSFTIP00000006214.1};
OS Falco tinnunculus (Common kestrel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Falconiformes; Falconidae; Falco.
OX NCBI_TaxID=100819 {ECO:0000313|Ensembl:ENSFTIP00000006214.1, ECO:0000313|Proteomes:UP000694562};
RN [1] {ECO:0000313|Ensembl:ENSFTIP00000006214.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSFTIP00000006214.1}
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; ENSFTIT00000006494.1; ENSFTIP00000006214.1; ENSFTIG00000004201.1.
DR Proteomes; UP000694562; Unplaced.
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; 3.40.1620.70:FF:000003; Collagen type XVIII alpha 1; 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; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1091; COLLAGEN ALPHA-3(IV) CHAIN-LIKE ISOFORM X1; 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:UP000694562};
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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1352
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034709150"
FT DOMAIN 32..220
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 217..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1097..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..236
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..287
FT /note="Polar 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 320..332
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..342
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 535..546
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 617..626
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..645
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..698
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..713
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..762
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..805
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..858
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..931
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 936..945
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..977
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1001
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1023
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1352 AA; 137725 MW; AB4D6D3634D2A6B3 CRC64;
MRPGCPPRPL LLGFFVLLVP TASQEPEDLS ADVSLLELIG DPPPEEILKI YGPDNNPGYV
FGPNANTGQV ARYHLPSPFY RDFSLLFHIQ PTTPRAGVLF AVTDSSQSII YVGVKLSELQ
AGKQQIIFYY TEPGSPSSYA AATFTVPTLL NQWTRFAISV EEDEVILYLD CEEHERVRFE
RSPDEMELED GSGLFVAQAG GADPDKYQGV IADLKLQGDP RAAERQCEEE EDDTEVSGDF
GSGAEGGHQP SGKVGGVPGL VDAIPVNSPP VAAGNRPRSS GGSPQQAERT RAEETLRVST
GGTGPKGEKG EKGERGLKGD SGTSGIVGTG SVKGEKGEKG ELGVKGSAGF GYPGSKGQKG
EPGDPGPPGT LSRHADGSVV EQVTGPPGPP GKDGAPGRDG EPGDPGEDGK PGDMGPQGFP
GTPGEPGLKG EKGDPGVGPR GPPGPPGPPG PPGPSSKHDK LTFIDMEGSG FGSDLESLRG
PRGPPGPPGP PGVPGLPGEP GRFGMNRTDL PGPPGLPGRD GIPGPPGPAG PQGPPGRDGA
AGQPGPKGEQ GDIGDLGLPG VPGPKGSKGE TGPAGAPGEM GLAGLPGPIG PRGQPGPPGP
PGPPGPGYEA GFGDMEGSGL PFTSGSPGPP GPEGPQGVPG LPGVKGEVGS PGQPGLPGPK
GDAGVPGVDG RPGLEGFPGP QGPKGDRGSP GDKGERGQDG VGLPGPPGPP GPPGQVITLS
SEDKSLAVLP GPEGRPGHAG FPGPVGPKGD QGSSGPQGPP GLKGEKGEPG VIISPDGTVV
TAKVKGEKGE PGLRGPMGPL GPQGRAGMKG EIGFPGRPGR PGMNGLKGEK GDPADVSSML
GLRGPPGPPG PPGPPGPPGS IVYDSSNAFS DSGHPMLPAF PGFHQLPGQK GEKGDPGAPG
PPGHFPYDPS HFGANLRGDK GDAGPKGEKG EPGSTPLYGP SVSGLPGPPG PQGYPGLPGP
KGDSIVGPPG PPGPQGPPGI GYEGRQGPPG PPGPPGPPSF PGPHRQAISI PGPPGPPGPP
GPPGTSTVSL GLRALPTYQA MLSSANELPE GSLVFLTDRQ ELYVRLRGGF RRVLLEEHNL
IPSSALDNEV YDKPPSVHYA GAQSPLQPRG PLHPLRNHGL PPTARPWRGD EVVANQHRLP
EQPLLHHQHE LLNSYYIHRR PDPAPVAAHV HQDFQPALHL VALNAPLSGG MRGIRGADFQ
CFQQARQVGL AGTFRAFLSS RLQDLYSIVR RADRAAVPIV NLRDEVLFSN WEALFTGSGA
PLRAGARILS FDGRDVLRDA GWPQKSVWHG SDAKGRRLPE SYCETWRTEE RTATGQASSL
GSGKLLEQVA SSCQHTFVVL CIENSFMTAA KK
//
