ID A0A8B9RV79_9AVES Unreviewed; 1127 AA.
AC A0A8B9RV79;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 20.
DE SubName: Full=Collagen type XVIII alpha 1 chain {ECO:0000313|Ensembl:ENSANIP00000013118.1};
OS Accipiter nisus (Eurasian sparrowhawk).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Accipitrimorphae;
OC Accipitriformes; Accipitridae; Accipitrinae; Accipiter.
OX NCBI_TaxID=211598 {ECO:0000313|Ensembl:ENSANIP00000013118.1, ECO:0000313|Proteomes:UP000694541};
RN [1] {ECO:0000313|Ensembl:ENSANIP00000013118.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSANIP00000013118.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
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DR Ensembl; ENSANIT00000013587.1; ENSANIP00000013118.1; ENSANIG00000008907.1.
DR Proteomes; UP000694541; Unplaced.
DR GO; GO:0005581; C:collagen trimer; 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; 3.40.1620.70:FF:000003; Collagen type XVIII alpha 1; 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; IPR016187; CTDL_fold.
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 SUPFAM; SSF56436; C-type lectin-like; 2.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Reference proteome {ECO:0000313|Proteomes:UP000694541};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 820..860
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 953..1122
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 68..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 871..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..115
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..241
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..281
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..309
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..321
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..333
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..390
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..403
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..485
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..500
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..645
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..718
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..732
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..764
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..788
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..810
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..893
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1127 AA; 114007 MW; AD957545744482C2 CRC64;
MRRTECPPWS RSWDAXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXFPF
PTMPAGTPVG TWWGGHPQTR PGPFSLPTGT GPKGEKGEKG ERGLKGDSGT GGIVGMGSVK
GEKGEKGELG IKGSAGFGYP GSKGQKGEPG EPGPPGTLSR HADGSVVEQV TGPPGPPGKD
GAPGRDGEPG DPGEDGKPGD MGPQGFPGTP GEPGLKGEKG DPGVGPRGPP GPPGPPGPPG
PFSKHDKLTF IDMEGSGFGG DLESLRGPRG PPGPPGPPGV PGLPGEPGRF GMNHTDLLGP
PGLPGRDGTP GPPGPAGPQG PPGRDGAAGQ PGPKGEQGDV GDLGLPGAPG PKGNKGEMGP
AGAPGEMGLA GLPGPIGPRG PPGPPGPPGP AGRGYEAGFG DMEGSGLPFT AGSPGPPGPE
GPQGVPGLPG VKGEVGSPGQ PGLPGLKGDA GIPGVDGRPG LEGFPGPQGP KGDRGSPGEK
GERGQDGVGL PGPPGPPGPP GQVITVSSED KSLVALPGPE GRPGHAGFPG PVGPKGDRGS
SGPQGSPGLK GEKGEPGVII SPDGTVVTAK VKGEKGEPGL RGPMGPSGPQ GRAGMKGEIG
FPGRPGRPGM NGLKGEKGDP ADVSSILGLR GPPGPPGPPG PPGPPGSIVY DSSNAFSDSS
HPALPAFPGF HQFPGQKGEK GDAGAPGPPG HFPYDLSHFS ASLRGDKGDA GPKGEKGESG
STPLYGPSIS GLPGPPGPQG YPGLPGPKGD SIVGPPGPPG PQGPPGMGYE GRQGPPGPPG
PPGPPSFPGP HRQAISIPGP PGPPGPPGPP GTSGMSLGLR TLPTYQAMLS AAHELPEGSL
IFLTDRQELY VRLRGGFRRV LDNEVYDKPP SIHYAGPQPP LQPRGPLHPL HNHSPPPTAR
TWHGDEVVAN QHRLPEQPLL HHQHELLNSY YIHRRPDPAP VVAHVHQDFQ PALHLVALNA
PLSGGMRGIR GADFQCFQQA RQVGLAGTFR AFLSSRLQDL YSIVRRADRA AVPIVNLRDE
VLFSNWEALF TGSGAPLRAG ARILSFDGRD VLRDVGWPQK SIWHGSDAKG RRLPESYCET
WRTEERAVTG QASSLGSGKL LEQMASSCQH AFVVLCIENS FMTAAKK
//
