ID A0A9W3G2P2_CAMBA Unreviewed; 1163 AA.
AC A0A9W3G2P2;
DT 08-NOV-2023, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2023, sequence version 1.
DT 28-JAN-2026, entry version 12.
DE SubName: Full=Collagen alpha-1(XV) chain isoform X1 {ECO:0000313|RefSeq:XP_045371192.1};
GN Name=COL15A1 {ECO:0000313|RefSeq:XP_045371192.1};
OS Camelus bactrianus (Bactrian camel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Camelus.
OX NCBI_TaxID=9837 {ECO:0000313|RefSeq:XP_045371192.1};
RN [1] {ECO:0000313|RefSeq:XP_045371192.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_045371192.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_045371192.1; XM_045515236.1.
DR AlphaFoldDB; A0A9W3G2P2; -.
DR CTD; 1306; -.
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 CDD; cd00247; Endostatin-like; 1.
DR FunFam; 3.40.1620.70:FF:000002; Collagen alpha 1 (XV) chain; 1.
DR FunFam; 3.10.100.10:FF:000008; collagen alpha-1(XVIII) chain isoform X1; 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; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1077; COLLAGEN ALPHA-3(IV) CHAIN; 1.
DR Pfam; PF01391; Collagen; 3.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 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 ECO:0000313|RefSeq:XP_045371192.1}.
FT DOMAIN 910..958
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 993..1158
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 108..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 770..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 814..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..279
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..364
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..385
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..408
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..509
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..618
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..662
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..698
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..723
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..839
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..882
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..901
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1163 AA; 118432 MW; 3072A191574AB58A CRC64;
MTHRWNRFAV VVQGEEVTLL VDCEEHSHVP FPRSSRALTF EPSAGIFVGN AGATGLERFT
GAIQQLTVHR DPRTPEMLCE AEDSSASGET SGLQETDEVA EILEAVTFTQ APSRETEVEP
INTPPTPSPP SEDTELSGEP VPKGTQETTN LSVILHGSPE QGSGEILNDT LERVHTVDGV
LVTDTGSGDR GFPDVIEEGS PTEEGLTATA AAEVPISTAR EAEVDIVPTG GPKLSTSTKD
SGEGVTLGPD DEEGSAATVA GEAEVPVSSA GEAEASSEPT RGLTFSMSIQ DPGEGVTLGP
GDEDSVAVAT EEPFMASGAE ELGGAPPEGP LLPVPTVAPE RGVPLGEAEE GLPGFPGSAG
PAGPTVGAEA EGSGLGWGLD VGSGSGDLVR SEELLRGPPG PPGPPGLPGL PGKPGTDVFI
GPPGSPGEDG PAGEPGPPGP EGKPGLNGAS GHPGMKGEKG ERGPNGSVGE KGDPGNRGLP
GPPGKNGQVG TPGVRGPPGP PGPPGPPGPG CATGLGFEDT EGSGSIRLLH EPRISGSTAS
SGPKGEKGDQ GPKGDRGMDG ASIVGPPGPR GPPGRIEVLS SSLVNITHGF MNLSDIPELV
GPPGPEGMPG LPGFPGPRGP KGDTGVPGFP GLKGEQGEKG EPGAILTGDV PLERLRGKKG
EPGAHGAPGP MGPKGPPGHK GEFGLPGRPG RPGLNGLKGA KGDRGVMMPG PPGLPGPPGP
PGPPGAVINI KGAIFPIPVR PHCKTLVGTT HPGNSELITF HGVKGEKGSW GLPGSKGEKG
VQGAQGPPGP PVDPTYLRHF LNSLKWENED REFKGVKGDS NSGFSVSGPP GLPGSPGLVG
QKGETVVGPQ GPPGVPGLPG PPGFGRPGSP GPPGPPGPPG PPAILGAAVA LPGPPGPPGQ
PGLPGTRNLV TALSNMDDML QKAHLVIEGT FIYLRDSTEF FIRVRDGWKK LQLGELIPIP
DDSPPPPALS SNPHQPQLPL MSVSSVSYGR PALHLVALNT PFSGDIRADF QCFQQARAAG
LLSTYRAFLS SHLQDLSTVV RKAERYSLPI VNLKGQVLFN NWESIFSGNG GQFNTHIPIY
SFDGRDVMTD PSWPQKVVWH GSNTHGVRLV DQYCEAWRTA DMAVTGLASA LSTGKILDQK
AYSCANRLIV LCIENSFMTD TRK
//
