ID A0A485MTV4_LYNPA Unreviewed; 1390 AA.
AC A0A485MTV4;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 28-JAN-2026, entry version 23.
DE SubName: Full=Type alpha isoform cra_a {ECO:0000313|EMBL:VFV23849.1};
DE Flags: Fragment;
GN ORFNames=LYPA_23C015714 {ECO:0000313|EMBL:VFV23849.1};
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:VFV23849.1, ECO:0000313|Proteomes:UP000386466};
RN [1] {ECO:0000313|EMBL:VFV23849.1, 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 -!- 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; CAAGRJ010005848; VFV23849.1; -; Genomic_DNA.
DR Proteomes; UP000386466; 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; 1.
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:UP000386466};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 141..329
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 1..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..1075
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1145..1164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..85
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..366
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..429
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..445
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..466
FT /note="Basic and acidic 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 539..549
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..583
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..593
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..603
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..638
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..655
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..744
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..761
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..887
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..903
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..931
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 956..976
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1000
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1046
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1068
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:VFV23849.1"
SQ SEQUENCE 1390 AA; 141022 MW; ED87512AB514406F CRC64;
SPASSRRAPP LPTSHRPEGL ACEPRGSPGW LVVLPTGRDV RPVQSGEAHP CPGAPGLAGI
QNPRSRSHTN RRTHIRAHGH RLARHGPRDI GASAAPSRKS VSPRVSHTSE VDHTRTSAPR
AGASTGAGVL FPLSEESPGT EVGLLQLLGE PPPQQVAQVD DPDVGPAFVF GPDANSGQVA
RYHFPSPFFR DFSLLFHVRP ATEGAGVLFA ITDAAQAVVS VGVKLSAVRD GQQHIQLLYT
EPGATRTRTA ASFRLPAFTG QWTRFALSVD GATVALFVDC ELFQRVPLVR SPRALELEPG
AGLFVAQAGG ADPSKFQGRI AELRVRGDPR VSGDFGSGLE ENRELLREQS GLSPKPSLPE
APPVTSPPLA GGRNVEDSRT EEIEEETTMS SLGAWTLPGS DTVTAWSVRS PGGGPEEGPA
GSAVQSPDAQ PVPGPQGPPG PPGPPGKDGA PGKDGEPGDP GEDGKPGDPG PQGFPGTPGD
MGPKGEKGDP GVGPRGPPGP QGPPGPPGPS FRHDRLTFID MEGSGFGGDL ESLRGPRGFP
GPPGPPGVPG LPGEPGRFGM NSSDVPGPAG LPGVPGRDGA PGLPGAPGPP GPPGRDGGPG
KTGQKGSPGE AGTPGPKGSK GDPGPTGAPG ETGLAGAPGP AGPPGPPGPP GPPGPGLAAG
FEDMDGSGGP FWSTAHGASG PQGPPGLPGV KGDPGIAGPP GAKGEVGADG PPGFPGLPGR
EGTAGAQGPK GEKGTQGEKG DPGRDGVGQP GLPGPPGPPG PVVYVSEQDR AVAGVPGPEG
RPGYAGFPGP AGPKGDLGSK GQRGPPGPKG EKGEPGPVFS PDGGTLGPAQ KGAKGEPGFR
GPPGPYGRPG HKGEIGFPGR PGRPGMNGLK GEKGEPGHGS VGFGVRGPPG PPGPPGPPGP
PGTPVYDSNA FMESGRPGPP GLPGYQGPPG PKGDKGEVGP PGPPGQFPLD LLQLEAEMKG
EKGDRGDPGQ KGERGEPGGG GFFGSSVPGP PGPPGYPGIP GPKGESIRGQ PGPPGPQGPP
GIGHEGRQGP PGPPGPPGPP GPPSFPGPYR QTISVPGPPG PPGPPGPPGT MGTSSGQVRI
WATYQTMLDK VPEVPEGWLI FVAETEELYV RVRNGFRKVL LEARTPLPRG TDNEVAALQP
PLVQLHEGNP YPRRELTHST ARPWRADDIL AGPPRLPDPR PYPGAPHHGP YLHVQPARPT
GGPARTHTHQ DFRPVLHLVA LNSPQPGGMR GIRGADFQCF QQARAVGLAG TFRAFLSSRL
QDLYSIVRRA DRTGVPVVNL RDEVLFPSWE ALFSGSEGQL EPGARVLSFD GRDVLQHPAW
PQKSVWHGSD PSGRRLTDSY CETWRTEDAA AAGQASSLLA GRLLAQKAAS CRNAFIVLCI
ENSFMTSSSK
//
