ID A0A803W7C8_FICAL Unreviewed; 1257 AA.
AC A0A803W7C8;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 28-JAN-2026, entry version 21.
DE SubName: Full=Collagen type XV alpha 1 chain {ECO:0000313|Ensembl:ENSFALP00000030884.1};
GN Name=COL15A1 {ECO:0000313|Ensembl:ENSFALP00000030884.1};
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:ENSFALP00000030884.1, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000030884.1, 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:ENSFALP00000030884.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSFALP00000030884.1}
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 AlphaFoldDB; A0A803W7C8; -.
DR Ensembl; ENSFALT00000033735.1; ENSFALP00000030884.1; ENSFALG00000013256.2.
DR GeneTree; ENSGT00940000164061; -.
DR Proteomes; UP000016665; Chromosome 2.
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: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; 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; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 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; 2.
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:UP000016665};
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..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1257
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5032444355"
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..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 861..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 951..998
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 710..719
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..811
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..884
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..975
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 985..994
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1257 AA; 129755 MW; 0E798F78E17A7DD5 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 PGPVIAIPEG PRGPKGDTGL PGLQGPKGQQ
GEKGEPGAII SADGSLTELL GRKGEKGEAG VVGPAGPMGP IGPTGPKGEL GLPGRPGRPG
LNGLRGAKGD RGEAVNGPPG LPGPPGPPGP PGRILYIKGT VFPVPPRPHC KMPVNTPYPG
NQEVLNDHGA RANRDSWGLH SSAHLKGEKG DRGAPGPPGP PLPPSYFSHF INSIKGEKGD
NGVTGVKGEK GEPNGGFFLT GPPGPPGRPG IIGPKGDSVV GPRGPPGLPG LPGLPGYGKI
GPPGPPGPPG PPGPPAIYGS AAAMPGPPGP PGEPGSPATR NLVTTFQNIE GMLEKVHYVA
EGTLIYLRET SEVFIRVRKG WRKLQLGELI PIPADSLPPP AISSHGFQSI PALRPISNMN
RRKPALHLVA LNFPLSGDMR ADFQCFRQAQ LAGLTSTYRA FLSSHLQDLA TVVRKTDRQH
LPVVNLQGET LFSNWESIFD GNGGQFNTHV PIYSFDGRNV MTDSSWPQKI IWHGSTANGI
RLVSNYCEAW HTADMGAMGQ ASPLNTGKLL DQKVYSCNNL FIVLCIENSF VSDPQGK
//
