ID W5MXD5_LEPOC Unreviewed; 1213 AA.
AC W5MXD5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 28-JAN-2026, entry version 66.
DE SubName: Full=Collagen, type XV, alpha 1b {ECO:0000313|Ensembl:ENSLOCP00000013044.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000013044.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000013044.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSLOCP00000013044.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
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; AHAT01017572; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01017573; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01017574; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01017575; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01017576; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01017577; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01017578; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01017579; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01017580; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5MXD5; -.
DR STRING; 7918.ENSLOCP00000013044; -.
DR Ensembl; ENSLOCT00000013072.1; ENSLOCP00000013044.1; ENSLOCG00000010624.1.
DR eggNOG; KOG3546; Eukaryota.
DR GeneTree; ENSGT00940000164061; -.
DR HOGENOM; CLU_004003_1_0_1; -.
DR InParanoid; W5MXD5; -.
DR OMA; RATEDQC; -.
DR Proteomes; UP000018468; Linkage group LG9.
DR Bgee; ENSLOCG00000010624; Expressed in camera-type eye and 13 other cell types or tissues.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0001501; P:skeletal system development; IBA:GO_Central.
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; 6.
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:UP000018468};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 9..197
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 197..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 845..938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..307
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..332
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..387
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..429
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..478
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..531
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..567
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..854
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..913
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..937
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1213 AA; 124728 MW; 45E47FB43836BB09 CRC64;
MEERGSKGHI DLTALIGVPL PPSVSFITGY EGFPAYSFGP NANIGRLTKT FIPDPFYKDF
AIIVTIKPTT NRGGVLFAIT DAFQKIVHLG LSLTPVEDKT QRIIMYYTEP GASRSRQVAS
FKVPGMTNKW SRFTLTMQDN EVTLYMDCED YHRVTFQRTT DQLQFESSSG IFVGNAGGTG
LEKFVGSIQQ LLIKPDPRAA EEQCEEDDPY ASGSGDDALL DGDTVDEVKK QVRELARPVP
APPTESSEDT DNYSGNLVEE AVEEAHTPNV VLAEERVNLK PAGAIYSQKG ERGDPGPRGP
PGPPGPPGET RTAEGQPGPR GPPGLRGTAG PPGKDGQPGI PGKDGTPGEK GPQGFPGLPG
ESGAKGEKGD PGVGLPGPPG PPGPPSPARF LSGADGYGSG FGDFDSDAEV IRGPPGPPGP
PGKPGPPGPS VSLDASAALL PGPPGLPGTP GQDGKDGQIG KPGLPGPPGR DGGVGPQGEK
GEKGNPGLAG PRGPKGDAAE PGMTGPTGLP GSNGERGLPG PQGPPGPPGP PGRGYSFEDM
EGSGRLGPIG EPGMRGPPGS PGLPGSPGPK GAAGLDGQPG EKLSLQGDPG TPGLDGKPGL
AGLPGPRGEK GEKGSQGPKG EPGQDGKSIT GPPGPPGPPG DIISLQEILH YSTVIYLWVF
PVLYSPGLQG PEGMPGRAGF PGPRGPKGDI GFPGIQGPPG LKGEKGEPGV TIAADGSLMS
GLRGPQGPKG VKGDRGFPGP IGVMGPEGRP GLKGEFGFPG RPGRPGMVGK KGEKGEAVVL
PGPPGPPGPP GPPGAVLGLK GTSLQNTRFQ GPKGDKGEVG FPGKPGIAGP WFPKGFVGDK
GDIGYKGEKG EKGEAGIPGP PGLPGRSGLV GPKGESIIGP QGLPGMPGQP GPPGFGRPGP
QGPAGPPGPP GPPALYGSAV SIPGPPGPPG LPGPPGIGNP VTTYRSLETL LKETYRTAEG
TMAYIADKSE VYIRVREGWR KIQLGELIPI PADSPSSHVS SGLYNPFLNI KLIFLQELQS
FLPGYSLLPH TIHTTPGLHL VALNAPFSGD MHGIRGADFQ CFQQARAMGL MATYRAFLSS
HLQDLATVVK KADRFTMPIV NLRGDVLFNN WMSIFSGNGG QFDPQIPIYS FDGRNVMTDP
SWPQKMVWHG SSPIGIRLTS NYCEAWRAGD MAVTGQASLL HSGRLLDQHT RSCSNNFIVL
CIENSYVQNQ RRK
//
