ID A0A485MX37_LYNPA Unreviewed; 1377 AA.
AC A0A485MX37;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 28-JAN-2026, entry version 25.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0000256|ARBA:ARBA00074723};
GN ORFNames=LYPA_23C017220 {ECO:0000313|EMBL:VFV22582.1};
OS Lynx pardinus (Iberian lynx) (Felis pardina).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Lynx.
OX NCBI_TaxID=191816 {ECO:0000313|EMBL:VFV22582.1, ECO:0000313|Proteomes:UP000386466};
RN [1] {ECO:0000313|EMBL:VFV22582.1, ECO:0000313|Proteomes:UP000386466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Alioto T., Alioto T.;
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Restin potently inhibits angiogenesis.
CC {ECO:0000256|ARBA:ARBA00058706}.
CC -!- FUNCTION: Structural protein that stabilizes microvessels and muscle
CC cells, both in heart and in skeletal muscle.
CC {ECO:0000256|ARBA:ARBA00058695}.
CC -!- SUBUNIT: Interacts moderately with EFEMP2.
CC {ECO:0000256|ARBA:ARBA00065596}.
CC -!- SUBUNIT: Trimer; disulfide-linked. {ECO:0000256|ARBA:ARBA00061770}.
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 EMBL; CAAGRJ010004677; VFV22582.1; -; Genomic_DNA.
DR Proteomes; UP000386466; Unassembled WGS sequence.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-ARBA.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
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; 3.40.1620.70: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 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; IPR001791; Laminin_G.
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; 3.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SMART; SM00282; LamG; 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, ECO:0000313|EMBL:VFV22582.1};
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:UP000386466};
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..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..1377
FT /note="Collagen alpha-1(XV) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019800146"
FT DOMAIN 44..232
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 93..231
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 227..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 827..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 980..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1021..1117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1173..1195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..599
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..622
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..723
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..772
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..876
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1021..1036
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1096
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1106..1115
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1377 AA; 140374 MW; F1C0E7F7B6BD5CB0 CRC64;
MADRLCRTVR NGRWWPLLLL LSVSALLPSV TRTRSATESL SPGHLDLTEL IGVPLPSSVS
FVTGYGGFPA YSFGPGANVG RPARTLIPPT FFRDFAITVT VKPSSATGGV LFAITDAFQK
VIYLGLRLSG VEDGRQRIIL YYTEPGSHVS HEAAAFLVPV MTHRWNRFAV IVQGEEVTLF
MDCEEHSHVP FQRSSRALAF EPSAGIFVGN AGATGLERFT GSIQQLTVHP DPRTPEELCE
ADESSGSGET SGLQETEGVA EILEAVTYTQ APSKEAKVEP INTPPTPSTP SDDGELSGEP
VPEGTPETTN LSVILHSSPE QGSGEILNDT LEGVHTVDGA PVTDVGSGDG TLIHVTEESV
HTEEGLAATA AAGEAEVPIS TTGEAEASSA PTGGPALSLS TEDMGEGVTP GADAEEGSAA
TAAEEAEVPI STAGEVEAGS VPTAEVTLSV STQGPGERVT LGPVGEETLT TAAAAAEASL
STSEEEEARG VPTDGLAPLA PTAAPEQEVT SGPGDEEDLA AASTEEPIPV AVAEELDSTL
PEGPPLPVPT VASERTVTPG EAGEGLPGHP EPVRPTAATV SAEAEGSGLG WGSDIGSGSG
DLVRTEELLR GPPGPPGPPG SPGIPGKPGT DVFMGPPGSP GKDGAAGEPG PPGPEGQPGP
DGASGLPGMK GEKGARGPNG SAGEKGDPGS RGLPGPPGKN GQVGAPGVMG PPGPPGPPGP
PGPGCAMGLG FEDTEGSGSI RLLHEPRISG PAVSSGPKGE KGDQGPKGDR GMDGASIVGP
PGPRGPPGRI EVLSSSLVNI THGFLNLSDI PELIGPPGPE GIPGLPGFPG PRGPKGDTGV
PGFPGLKGEQ GEKGEPGAIL TGDIPLERLQ GRKGEPGVHG APGPMGPKGP PGHKGEFGLP
GRPGRPGLNG LKGAKGDRGV MMPGPPGLPG PPGPPGPPGA VINIKGAVFP IPVRPHCKTP
VDTTHPGNSE LITFHGVKGE KGSWGLPGSK GEKGDQGAQG PPGPPVDPTY LRYLLNSLKG
ENGDRGIKGE KGDSHGDFFV SGPPGLPGSP GLVGQKGETV VGPQGPPGAP GLPGPPGFGR
PGSPGPPGPP GPPGPPAILG AAVALPGPPG PPGQPGLPGS RNLVTAFSSM DDMLQKAHLV
IEGTFIYLRD STDFFIRVRD GWKKLQLGEL IPIPEDSPPP PALSSNPHQP QPPLMSLSSV
NYQRPALHLV ALNTPFSGDI RADFQCFQQA RAAGLLSTYR AFLSSHLQDL STVVRKAERY
NLPIVNLKGQ VLFNNWDSIF SGHGGQFNTH VPIYSFDGRD VMTDPSWPQK VIWHGSSTHG
VRLVDKYCEA WRTADMAVMG LASPLSTGKI LDQKAYSCAN RLIVLCIENS FMTDARK
//
