ID A0A6J2VF37_CHACN Unreviewed; 1314 AA.
AC A0A6J2VF37;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 28-JAN-2026, entry version 23.
DE SubName: Full=Collagen, type XV, alpha 1b {ECO:0000313|RefSeq:XP_030630552.1};
GN Name=col15a1b {ECO:0000313|RefSeq:XP_030630552.1};
OS Chanos chanos (Milkfish) (Mugil chanos).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Gonorynchiformes;
OC Chanidae; Chanos.
OX NCBI_TaxID=29144 {ECO:0000313|Proteomes:UP000504632, ECO:0000313|RefSeq:XP_030630552.1};
RN [1] {ECO:0000313|RefSeq:XP_030630552.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (AUG-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 RefSeq; XP_030630552.1; XM_030774692.1.
DR GeneID; 115812209; -.
DR CTD; 558137; -.
DR InParanoid; A0A6J2VF37; -.
DR OrthoDB; 10060752at2759; -.
DR Proteomes; UP000504632; Chromosome 5.
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 ECO:0000313|RefSeq:XP_030630552.1};
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:UP000504632};
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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1314
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5026926993"
FT DOMAIN 90..278
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 60..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 809..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1095..1114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..399
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..482
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..537
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..623
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..665
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..675
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..715
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..733
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..859
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..883
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 914..923
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..954
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1012
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1032
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1314 AA; 134757 MW; 02E7770EE1CF6BBE CRC64;
MAGGAPSLCL LSLLCLAAPA QGQWWAFFWG KGITTPAPVN TPAPTTGVTE ETTLSVLLTT
PPVPTENGAS KPRPKRPLKM WKSERGSKDH LDLTHLIGVP LPPFVSFMTG YEGFPAYSFE
PEANIGRLTK SFVPDPFFRD FAIIVTVKPT NTNGGVIFAI TDAPQQVVHL GLALTPVEDH
TQRILLYYSE PGATHTQQVA SFKVPDMTQK WSRFTLAVQD EEVRLDMDCE EYHTTAFQRG
PRPLSFEPGS GIFVANAGGT GLEKFVGCIQ QLIIKPDPRA AEEQCEEDDP YVSGDGSGYD
GLDDRETEDE LMKREKDSKH ISWPGYDLSE PVHAPPTMPP ELEGEEYSGH LTPTEESRHK
MQFRGEKCSG DRIGQKGERG EPGPAGPPGL PGPPGPALPP KERALAGPPG PRGPKGPAGA
PGRPGKDGQP GSKGEDGKPG ERGLPGYPGP PGESGVKGEK GDPGMAIPGP PGPPGPPGPP
GLSRPAKYPE GLDAFGSGLG DLDGDAELII RGPPGPPGPP GQPGPPGPSI PFKPLLPGPT
GLPGIPGKDG RDGLIGKPGL PGVPGQDGAQ GPKGEKGDPG KIGTPGPKGE AGEPGLNGQP
GPVGPMGEKG EPGPPGPPGP PGPSANGFML EDLEGSGREG VIGTGVLKGS QGPPGLPGEP
GPQGPPGADG APGLSVKGEP GAPGPDGMPG LAGLPGARGQ KGEKGSPGPK GERGQDGLNI
TGPPGPPGPP GPPISIQDLL LNDTRGIFNF SEIRGPPGPM GPEGLPGRAG FPGPRGPKGD
IGFPGVQGPP GLKGDKGEPG VAIAADGSIM TGLRGPRGPK GARGDRGLPG PAGLTGPIGP
TGPKGEYGIP GRPGRPGIAG KKGDKGESVG LPGPPGPPGP PGLPGRIIGL NGTVFPVRPR
PHCKQTINNN KEGPQGEKGD KGDLGYPGTP GSPGKAIGEK GDHGYKGQKG EKGDPGLPGP
PGLPGRSGLV GPKGESVVGP PGKPGTPGQP GQPGFGRPGP RGPPGPAGPP GAPSHNTAAA
SIPGPPGPPG LPGAPGHGSP VTTFKSVQIL MKETHSSTEG TIAYISDKSE LYIRVRSGWR
KIPLGVLIPI PADSPDSAVS QGLSRPSERS TPRVHSQELQ SGLPGFSILT QHSLSVPGLH
LVALNAPLSG DIRGIRGADF QCYQQARAVG LTSTYRAFLS SHLQDLSSIV KKGDRINMPI
INLKGEMLFN SWLSMFSGNG AIFDPLVPIY SFDGRNVMTD ETWPQKLVWH GSSTQGIRLT
TNYCEAWRAG DMAVTGQASL LQTGRLLGQH TRSCSNHFIV LCIENSYVRD PRRP
//
