ID A0A8C9UHD6_SERCA Unreviewed; 1290 AA.
AC A0A8C9UHD6;
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:ENSSCAP00000021905.1};
GN Name=COL15A1 {ECO:0000313|Ensembl:ENSSCAP00000021905.1};
OS Serinus canaria (Island canary) (Fringilla canaria).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Passeroidea; Fringillidae; Carduelinae; Serinus.
OX NCBI_TaxID=9135 {ECO:0000313|Ensembl:ENSSCAP00000021905.1, ECO:0000313|Proteomes:UP000694409};
RN [1] {ECO:0000313|Ensembl:ENSSCAP00000021905.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSSCAP00000021905.1}
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; ENSSCAT00000024405.1; ENSSCAP00000021905.1; ENSSCAG00000015735.1.
DR GeneTree; ENSGT00940000158302; -.
DR Proteomes; UP000694409; Unassembled WGS sequence.
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; 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:UP000694409};
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..1290
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034991790"
FT DOMAIN 38..226
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 223..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 869..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 977..1033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..407
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..433
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..479
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..500
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..578
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..692
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..735
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..818
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 878..887
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..917
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1008
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1018..1027
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1290 AA; 133015 MW; C92D9E36D8B7055D CRC64;
MLSWHAWWTW DLSLLLFGLS IHAGAAAQII EERGSKGHLD LTELIGVPLP PSVYFVTGYG
GFPAYSFGPD SNIGRLTSAI IPSPFYRDFA VVVTVKPNSD RGGVLFAITD AFQKTIYLGL
RISPVDDSTQ RIIMYYTEPG SHISREAASF KVPVMTNRWN KFTVTVEGND IALFMDCEEY
QRLHFQRPAR TLVFESGSGI FVGNAGATGL EKFTGSIQHL TIKSDPRATE DHCEDDDPYA
SGDSSGNGSI QEYDSSEAQE ALAPSRLPIR PEDTLAEPVE APPTILAYLE ENDFSGNHRS
EETSEAAKSK EQAVMETGQG SSESTTVTQQ MLREEDGSGA GVLPGVSREE DQKGQEVEDG
STESLGGSGI EDVENKAQGP PGSPGKLGQL GQPGKNGLQG LPGLKGKAGP KGEKGDPGEG
LPGPPGLPGP TGPSAPSRGL NRLEPEESGS GDTDRETEIL RGLPGPPGPP GLPGLPGNPA
PDSGVGPPGS PGEDGASGEP GPEGPQGPPG RDGVAGPPGW KGEKGDQGLP GSAGPKGDTG
VRGSIGPKGE AGPIGSPGKP GPPGPPGPPG PPGPPGPPGL SYSLGFEDME GSASIDLLSE
PRIPRPRGPK GSAGRPGQRG PLGPKGERGN IGPPGAKGMP GTDGKPGFPG IAGHPGEVGP
KGEKGDPGPR GEPGQDGNSI VGPPGPPGPP GPVIAIPELL LNDTDGISNF TEIKGLLGPP
GPDGKPGLPG FPGPRGPKGD TGLPGSRGPK GQQGEKGEPG AIISADGSLT EFLGRKGEKG
EAGVMGPAGP MGPIGPTGPK GELGFPGRPG RPGLNGLRGV KGDRGEAFNG LPGLPGPPGP
PGPPGRILYI KGTVFPVPPR PHCKMPVNLP SPGNQEVLND HGAKANRDSW GLHSSAHLKG
EKGDRGAPGP PGPPLPPSYF SHFINSIKGE KGDNGVTGVK GEKGEPNGGF FLTGPPGPPG
RPGLIGPKGD SVVGPRGPPG LPGLPGLPGY GKIGPPGPPG PPGPPGPPAI YGSAAAMPGP
PGPPGEPGSP ATRNLVTTFQ NIEGMLEKVH YVAEGTLIYL RETSEVFIRV QKGWRKLQLG
ELIPIPADSL PPPAISSHGF QSIPALRPIS NMNNRKPALH LVALNFPLSG DMRADFQCFR
QAQLAGLTST YRAFLSSHLQ DLATVVRKAD RHHLPVVNLQ GETLFSNWES IFDGNGGQFN
VHVPIYSFDG RNVMTDSSWP QKIIWHGSTA NGIRLVSNYC EAWHTADMGA MGQASPLNTG
RLLDQKVYSC NNQFIVLCIE NSFVSDPQGK
//
