ID U3KFQ7_FICAL Unreviewed; 1299 AA.
AC U3KFQ7;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 28-JAN-2026, entry version 71.
DE SubName: Full=Collagen type XV alpha 1 chain {ECO:0000313|Ensembl:ENSFALP00000013861.2};
GN Name=COL15A1 {ECO:0000313|Ensembl:ENSFALP00000013861.2};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000013861.2, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000013861.2, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000013861.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSFALP00000013861.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR STRING; 59894.ENSFALP00000013861; -.
DR Ensembl; ENSFALT00000013918.2; ENSFALP00000013861.2; ENSFALG00000013256.2.
DR eggNOG; KOG3546; Eukaryota.
DR GeneTree; ENSGT00940000164061; -.
DR HOGENOM; CLU_004003_1_0_1; -.
DR Proteomes; UP000016665; Chromosome 2.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR CDD; cd00247; Endostatin-like; 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; 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; 3.
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 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Reference proteome {ECO:0000313|Proteomes:UP000016665};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1299
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5032900633"
FT DOMAIN 38..226
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 223..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 780..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 895..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 967..1034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..358
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..418
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..447
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..492
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..531
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..591
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..614
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..670
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..693
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..736
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..753
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..819
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..845
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..918
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1009
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1028
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1299 AA; 134348 MW; 51EFE5D555513C4A CRC64;
MLSWHAWWTW DLLLLLFGLS IHAGAAAQII EERGSKGHLD LTELIGVPLP PSVYFVTGYG
GFPAYSFGPD SNIGRLTSAM VPSPFYRDFA VVVTAKPNRD RGGVLFAITD AFQKTIYLGL
RISPVEDSTQ RIIMYYTEPG SHISREAASF KVPVMTNRWN KFTVAVEGND VALFMDCEEY
QRLHFQRSAR ALVFEAGSGI FVGNAGATGL EKFTGSIQHL TIKSDPRATE DHCEDDDPYA
SGDSSGNGSI QDHDISEAQE ALAPSRLPVR PEDTLAEPVE APPTILSYLE ENDFSGNHRT
EETSEAAKFK EQDSAVMETG QGDSESSPVT QRMLREEDGS GAGVLPGVSR EEGQKGQEVE
DGSTESLGGS GIEDVENKDQ GPPGSPGKPG QLGQPGIPGK NGLPGKNGLQ GLPGLKGKAG
PKGEKGDPGE GLPGPPGLPG PTGPPAPSRG LNRLEPEESG SGDTESIRET EILRGLPGPP
GPPGLPGLPG KPAPDSGVGP PGSPGEDGPS GEPGPEGPQG PPGRDGVVGP PGWKGEKGDQ
GLRGSAGPKG DTGVTGSMGP KGEAGPIGSP GKPGPPGPPG LPGPPGPPGP PGLSYGLGFE
DMEGSGSIEL LSESRIPVSR GPKGSVGRPG ERGPLGPKGM PGTDGKPGFP GIAGYPGEVG
PKGEKGDPGP RGEPGQDGNS VVGPPGPPGP PGPVIAIPEL LLNDTDGIFN FTESKRLLGP
PGPDGKPGLP GFPGPRGPKG DTGLPGLQGP KGQQGEKGEP GAIISADGSL TELLGRKGEK
GEAGVVGPAG PMGPIGPTGP KGELGLPGRP GRPGLNGLRG AKGDRGEAVN GPPGLPGPPG
PPGPPGRILY IKGTVFPVPP RPHCKMPVNT PYPGNQEVLN DHGARANRDS WGLHSSAHLK
GEKGDRGAPG PPGPPLPPSY FSHFINSIKG EKGDNGVTGV KGEKGEPNGG FFLTGPPGPP
GRPGIIGPKG DSVVGPRGPP GLPGLPGLPG YGKIGPPGPP GPPGPPGPPA IYGSAAAMPG
PPGPPGEPGS PATRNLVTTF QNIEGMLEKV HYVAEGTLIY LRETSEVFIR VRKGWRKLQL
GELIPIPADS LPPPAISSHG FQSIPALRPI SNMNRRKPAL HLVALNFPLS GDMRADFQCF
RQAQLAGLTS TYRAFLSSHL QDLATVVRKT DRQHLPVVNL QGETLFSNWE SIFDGNGGQF
NTHVPIYSFD GRNVMTDSSW PQKIIWHGST ANGIRLVSNY CEAWHTADMG AMGQASPLNT
GKLLDQKLSE LGIVRQLRQS NFQSVDPIIL KFMFPSKEV
//
