ID A0AA35PKV2_9SAUR Unreviewed; 1297 AA.
AC A0AA35PKV2;
DT 24-JAN-2024, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2024, sequence version 1.
DT 28-JAN-2026, entry version 11.
DE SubName: Full=Collagen alpha-1(XV) chain isoform X2 {ECO:0000313|EMBL:CAI5789610.1};
GN ORFNames=PODLI_1B002373 {ECO:0000313|EMBL:CAI5789610.1};
OS Podarcis lilfordi (Lilford's wall lizard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Laterata;
OC Lacertibaenia; Lacertidae; Podarcis.
OX NCBI_TaxID=74358 {ECO:0000313|EMBL:CAI5789610.1, ECO:0000313|Proteomes:UP001178461};
RN [1] {ECO:0000313|EMBL:CAI5789610.1}
RP NUCLEOTIDE SEQUENCE.
RA Alioto T., Alioto T., Gomez Garrido J.;
RL Submitted (DEC-2022) 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}.
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 EMBL; OX395138; CAI5789610.1; -; Genomic_DNA.
DR Proteomes; UP001178461; Chromosome 13.
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:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 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, ECO:0000313|EMBL:CAI5789610.1};
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:UP001178461};
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..1297
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041421874"
FT DOMAIN 38..226
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 221..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 877..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 966..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..403
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..455
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..498
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..510
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..520
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..594
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..688
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..711
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..753
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..776
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..835
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..976
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..1019
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1028..1037
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1297 AA; 133160 MW; E045C02FCEE45F72 CRC64;
MLPSHSRVPW NLLLLLLGSL LPAGLPAQVI EERGSKEHLD LTELIGVPLP PSVSFITGYG
GFPAYSFGPE ANIGRLTRTL IPQPFYRDFA IAVTVKPNSD RGGVLFAVTD AFQKTIYLGA
RLSSVDDSTQ RIIMYYTEPG SHISREAASF KVPVMTNKWN RFTIAVQGND IALFMDCEEY
HRVQFQRSDQ PLLFESSSGI FVGNAGATGL ERFTGSIQQL TIKPDPRATE DQCEDDDPYA
SGESSGYNSI QEQEGVPETQ EIIRPSQAPH LTQNVSEETT AGPVGAPPTT APHSEEMEFS
GHHLLEATLG PTKVQEQGLT TTEIRKQESE LTTMAQEILQ TTPEPRDGFL QVTGREKGQK
GEKGERGEEG PPGPPGKAGL DEAEPGTAGQ PGLPGKPGLD GKPGISGKDG LPGKPGLQGS
PGLKGEPGLK GEKGDAGIGL PGPPGLPGPP GPPAPSRGFR RVEMEASGSG DSDRDMEFPR
GAPGPPGPPG LPGAPGLPAP DSNAGIPGLP GENGKGGAAG HPGPRGPPGR PGQDGLAGSA
GAKGEKGDQG IWGSPGSKGD PGDIGLPGTK GADGEPGKPG IPGLPGPPGP PGPPGSGYGF
GFEDMEGSGI VGLSREPGTS RPSGRNGPAG EAGLQGPMGP KGEKGDNGLP GTPGLKGEQG
PEGRPGFPGV AGRPGDTGSK GDKGDPGPKG EPGQDGASVV GPPGPPGPPG PIIAIPRSLN
ASDESFNITR IKGLVGPPGP DGKPGLPGFP GPRGPKGDIG LPGSPGEKGK QGEKGEPGAI
FASAESLTEV IRRPGEKGEP GVTGPVGPMG PPGPSGLKGE LGFPGRPGRP GLNGKKGIKG
ERGVTLYGPP GVRGLPGPPG PPGRVVFIKG TVFPISPRPQ CKTTADTPHP GNPKVADEAD
SWSVSGPPVI KGEKGDRGAP GPPGPPLPST YFSQLNIMKG EKGVNGEVGL KGEKGEPNGG
FFMSGPPGLP GRPGPVGPKG DTVVGPRGPP GVPGLPGPPG FGPVGPPGPP GPPGPPGPPS
IYGSAAVPGP PGPPGEPGLP GTRNLVTRFR NVDTMLQKVH LVSEGTLIYL SETSEVFIRT
QGGWKKLQLG ELIPIPADSP PPPAISSPGF QPLPAPIPAS NTDVRRPSLH LVALNTPFSG
DMRADYQCFQ QARAAGLLST YRAFLSSHLQ DLLTVVRKAD RYHVPIVNLK GEPLFSNWES
IFSGNGGQFD LRIPIYSFDG RDVMTDPAWP QKVVWHGSSS NGIRLISNYC EAWRTADLAV
MGQASPLKSG KLLDQKAYSC SNRFITLCIE NSYVSDI
//
