ID A0A8C5JI32_JUNHY Unreviewed; 1298 AA.
AC A0A8C5JI32;
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 XV alpha 1 chain {ECO:0000313|Ensembl:ENSJHYP00000018705.1};
OS Junco hyemalis (Dark-eyed junco).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Passerellidae; Junco.
OX NCBI_TaxID=40217 {ECO:0000313|Ensembl:ENSJHYP00000018705.1, ECO:0000313|Proteomes:UP000694408};
RN [1] {ECO:0000313|Ensembl:ENSJHYP00000018705.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSJHYP00000018705.1}
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; ENSJHYT00000022574.1; ENSJHYP00000018705.1; ENSJHYG00000014226.1.
DR OMA; RATEDQC; -.
DR Proteomes; UP000694408; 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:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR Pfam; PF01391; Collagen; 4.
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:UP000694408};
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..1298
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034875967"
FT DOMAIN 38..226
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 221..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 984..1041
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..331
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 395..418
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..444
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..490
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..511
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..588
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..677
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..700
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..760
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..826
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..851
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..895
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..925
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1015
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1026..1035
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1298 AA; 133826 MW; 69748355D388A4FD CRC64;
MLSRHAWWTW DLSLLLFGLS IHAGAAAQII EERGSKGHLD LTELIGVPLP PSVYFVTGYG
GFPAYSFGPD SNIGRLTSAI IPSPFYSDFA IVATVKPNSD RGGVLFAITD AFQKTIYLGL
RISPVDDSTQ RIIMYYTEPG SRISREAASF KVPVMTNRWN KFTVTVEGNY IALFMDCEEY
QRLQFQRPAR TLVFESGSGI FVGNAGATGL EKFTGSIQHL TIKSDPRTTE DHCEDDDPYA
SGDSSGNGSI QEHDSSEAQE ALAPSHLPIR PEDSLAEPVE APPTILAYLE ENDFSGNHRS
EETSEAAKFK EQDLAVMETG QDNNESTTVT QKMLREEDGS GAGVLPGVSR EEGQKGQEVE
DGSTESLGGS GIEDVENKDQ GPPGSPGKLG QLGQSGIPGK NGSPGKNGPQ GLPGQKGKAG
QKGEKGDPGE GLPGPPGLPG PTGPSAPSRG VNRLEPEESG SGDTDRETEI LRGLPGPPGP
PGLPGLPGNP APDSGVGPPG SSGEDGASGE PGPEGPQGPP GRDGVAGPPG WKGEKGDQGL
PGSAGPKGDT GVTGSIGPKG EAGAIGSPGK PGPPGPPGPP GPPGPPGPSY SLGFEDMEGS
GSIDLLSESR IPRPREPKGS AGRPGQRGPL GPKGERVNIG PPGSKGMLGT DGKPGLPGIA
GHPGEVGPKG EKGDPGPRGE PGQDGNSIVG PPGPPGPPGP VIAIPELLLN ETGGISNFTE
IKGLLGPPGP DGKPGLPGFS GPRGPKGDTG LPGSQGPKGQ QGEKGEPGAI ISADGSLTEL
LGRKGEKGEA GVMGPVGPMG PIGPTGPKGE LGFPGRPGRP GLNGLRGVKG DRGEAFNGLP
GLPGPPGPPG PPGRILYIKG TVFPVPPRPH CKMPVNSPYP GNQEVLNDHG AKANRDSWGL
HSSAHLKGEK GDRGAPGPPG PPLPPSYFSH FINSIKGEKG DNGVTGVKGE KGEPNGGFFL
TGPPGPPGRP GLIGPKGDSV VGPRGPPGLP GLPGLPGYGK IGPPGPPGPP GPPGPHAIYG
SAVAMPGPPG PPGEPGSPAT RNLVTTFQNI EGMLEKVHYV AEGTLIYLRE TSEVFIRVQK
GWRKLQLGEL IPIPADSPPP PAISSHGFQS IPALRPVSYM NNGKPALHLV ALNFPLSGDM
RADFQCFRQA QLAGLTSTYR AFLSSHLQDL ATVVRKTDRH HLPVVNLQGQ TLFSNWESIF
DGNGGQFNIH VPIYSFDGRN VMTDSSWPQK IIWHGSTANG IRLVSNYCEA WHTADMGAMG
QASPLNTGKL LDQKVYSCNN QFIVLCIENS FVSDPQGK
//
