ID A0A665V7V5_ECHNA Unreviewed; 755 AA.
AC A0A665V7V5;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 25.
DE SubName: Full=Collagen, type XV, alpha 1b {ECO:0000313|Ensembl:ENSENLP00000027756.1};
OS Echeneis naucrates (Live sharksucker).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Echeneidae; Echeneis.
OX NCBI_TaxID=173247 {ECO:0000313|Ensembl:ENSENLP00000027756.1, ECO:0000313|Proteomes:UP000472264};
RN [1] {ECO:0000313|Ensembl:ENSENLP00000027756.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Wellcome Sanger Institute Data Sharing;
RL Submitted (APR-2021) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSENLP00000027756.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSENLP00000027756.1}
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}.
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 AlphaFoldDB; A0A665V7V5; -.
DR Ensembl; ENSENLT00000028593.1; ENSENLP00000027756.1; ENSENLG00000012425.1.
DR InParanoid; A0A665V7V5; -.
DR OMA; RATEDQC; -.
DR Proteomes; UP000472264; Chromosome 17.
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; 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; 2.
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:UP000472264};
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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..755
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025506325"
FT DOMAIN 32..221
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 270..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..313
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..328
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..412
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..472
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 755 AA; 80674 MW; DF71C1369F8D6325 CRC64;
MFQGWSLALH LFLLCWLAAA LQVIEDQGSG DHLDLTELIG VPLPPSVSFT PGYEGFPAYN
FGPEANIGRL TKTFVPGPFY RDFAIIVTVR PTSQRGGILF AITDARQKVV ELGLALTPVR
RGLQSILLYY TDQEEATHSH KAAAFSVPDM TDQWTRFTVS LTRDEVRLYM DCGEAERTTF
HRRPERLTFS HNSGIFVANA GRTGLDKFVG SIQQLVIKDD PRAAEEQCED DDPYVRHTHT
HTRTNLPWTL LAAMTATHTN DDIFVHDKEK AETKGQVRPG SKGEPGEPGP PGPPGPPGPT
SLPGLPQPGP RGPQGPSGTP GSPGQKGPRG PKGDKGPPGN QGPAGLKGEK GDPGVTIAAD
GSLLTAQRGP QGPKGIKVSG AKGDQGQRGQ KGEKGNAGLP GPPGLPGRPG PVGPKGESIV
GPPGPVGSPG LQGPPGIGVR GPRGHPGLPG PPGQAYGSDV PGPPGLPGPP GTPGYANLVN
TFKTIQALTR ESQWAAEGTL AYVSERGGEL YIRSRNGWRK IQLGELIQQG PSSSAVSQAL
SRTGEWSKPH RVHSQVRHTH SQPSYNVLPQ TFNAVPGLHL VALNAPLKGD MRGIRGADFQ
CYQQARSMGL MATYRAFLSS HLQDLATIVR KTDRTDMPVV NIRGEVLFSS WMSIFSGNGG
IFNPSIPIYS FDGRNIMTDS AWPEKLVWHG SSTAGIRLTS NYCEAWRTGD VAVMGQAALL
QTGRLLGQHT RSCSNHYIVL CIENTYVGNT HPRRT
//
