ID L8IK21_9CETA Unreviewed; 976 AA.
AC L8IK21;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 28-JAN-2026, entry version 46.
DE SubName: Full=Collagen alpha-1(XV) chain {ECO:0000313|EMBL:ELR55477.1};
DE Flags: Fragment;
GN ORFNames=M91_20271 {ECO:0000313|EMBL:ELR55477.1};
OS Bos mutus (wild yak).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=72004 {ECO:0000313|EMBL:ELR55477.1, ECO:0000313|Proteomes:UP000011080};
RN [1] {ECO:0000313|EMBL:ELR55477.1, ECO:0000313|Proteomes:UP000011080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=yakQH1 {ECO:0000313|Proteomes:UP000011080};
RX PubMed=22751099; DOI=10.1038/ng.2343;
RA Qiu Q., Zhang G., Ma T., Qian W., Wang J., Ye Z., Cao C., Hu Q., Kim J.,
RA Larkin D.M., Auvil L., Capitanu B., Ma J., Lewin H.A., Qian X., Lang Y.,
RA Zhou R., Wang L., Wang K., Xia J., Liao S., Pan S., Lu X., Hou H., Wang Y.,
RA Zang X., Yin Y., Ma H., Zhang J., Wang Z., Zhang Y., Zhang D., Yonezawa T.,
RA Hasegawa M., Zhong Y., Liu W., Zhang Y., Huang Z., Zhang S., Long R.,
RA Yang H., Wang J., Lenstra J.A., Cooper D.N., Wu Y., Wang J., Shi P.,
RA Wang J., Liu J.;
RT "The yak genome and adaptation to life at high altitude.";
RL Nat. Genet. 44:946-949(2012).
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
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DR EMBL; JH881267; ELR55477.1; -; Genomic_DNA.
DR AlphaFoldDB; L8IK21; -.
DR STRING; 72004.ENSBMUP00000008277; -.
DR Proteomes; UP000011080; 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 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; 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; IPR016187; CTDL_fold.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 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.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119, ECO:0000313|EMBL:ELR55477.1};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}.
FT DOMAIN 723..771
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 806..971
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 1..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..12
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..127
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..137
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..219
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..320
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..428
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..504
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..629
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..652
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..695
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..714
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 976
FT /evidence="ECO:0000313|EMBL:ELR55477.1"
SQ SEQUENCE 976 AA; 98399 MW; F4AE8179C4FBF7F9 CRC64;
ESEEGAAATA AGEAEEPVSI AREAEASSVP TGGLTLPMPT QDPGEMVTLS PISEEGSTTA
AAATDVPLGT FEEEEASGVP TNDLAFITPT VASEQGVTSG PGDEDLAAAT TEEPLTAAGA
DALGSTPPEG PPLPLPSVAP ESGAPPVSED FTSRRDGEAE EGFPGPPGPA VPTEPTVEVE
AEGSGLGWGL DVSSGSGDLV HSEELLRGPP GPPGPPGLPG IPGKPGTDVF MGPPGSPGED
GPTGEPGPPG PEGKPGLDGA SGLPGMKGEK GARGPNGSVG EKGDPGNRGL PGPPGKTGQV
GAPGVMGPPG PPGPPGPPGP GCTTGLGFED TEGSGSIRHL HEPISGPTAS SGPKGEKGDR
GPKGDRGMDG ASIVGPPGPR GPPGRIEVLS SSLTNITQGF MNFSDIPELV GPPGPEGMPG
LPGFPGPRGP KGDTGVPGFP GLKGEQGEKG EPGAILTGDI PLERLRGQKG EPGEHGAPGP
MGPRGPPGHK GEFGLPGRPG RPGLNGLKGA KGDRGVMIPG PPGLPGPPGP PGPPGAVINI
KGAVFPVPVR PHCKTPVGTT YSGNSELITF HGVKGEKGSW GLPGSKGEKG DQGPQGPPGP
PVDPAYLRHF LNSLKGENGD RGIKGEKGDS NSGFSGFSVS GPPGLPGSPG LVGQKGEAVV
GAQGPPGAPG LPGPPGFGRP GSPGPPGPPG PPGPPAILGA AVALPGPPGP PGQPGLPGSR
NLVTTFSNMD DMLQKAHLVI EGTFIYLKDS TEFFIRVRDG WKKLQLGELI PIPDDSPPPP
ALSSNPHQPQ LSLTSISNVN YGRPALHLVA LNTPFSGDIR ADFQCFQQAR AAGLLSTYRA
FLSSHLQDLS TVVRKAERYS LPIVNLKGQV LFNNWDSIFS GHGGQFNTHI PIYSFDGRDV
MTDPSWPQKV IWHGSSTHGV RLVDQYCEAW RTADMAVMGL ASPLNTGKIL DQKAYSCANR
LIVLCIENSF MTDARK
//
