ID A0A8M2BIM9_DANRE Unreviewed; 1259 AA.
AC A0A8M2BIM9;
DT 03-AUG-2022, integrated into UniProtKB/TrEMBL.
DT 03-AUG-2022, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE SubName: Full=Collagen, type XV, alpha 1b isoform X5 {ECO:0000313|RefSeq:XP_005171292.1};
GN Name=col15a1b {ECO:0000313|RefSeq:XP_005171292.1,
GN ECO:0000313|ZFIN:ZDB-GENE-070912-689};
GN Synonyms=cb491 {ECO:0000313|RefSeq:XP_005171292.1}, sb:cb491
GN {ECO:0000313|RefSeq:XP_005171292.1}, si:dkeyp-93c5.1
GN {ECO:0000313|RefSeq:XP_005171292.1}, wu:fb50f05
GN {ECO:0000313|RefSeq:XP_005171292.1}, wu:fc22d09
GN {ECO:0000313|RefSeq:XP_005171292.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|Proteomes:UP000000437, ECO:0000313|RefSeq:XP_005171292.1};
RN [1] {ECO:0000313|RefSeq:XP_005171292.1}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:XP_005171292.1};
RC TISSUE=Fibroblasts and whole tissue
RC {ECO:0000313|RefSeq:XP_005171292.1};
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_005171292.1; XM_005171235.6.
DR AlphaFoldDB; A0A8M2BIM9; -.
DR GeneID; 558137; -.
DR AGR; ZFIN:ZDB-GENE-070912-689; -.
DR CTD; 558137; -.
DR ZFIN; ZDB-GENE-070912-689; col15a1b.
DR OrthoDB; 10060752at2759; -.
DR Proteomes; UP000000437; Chromosome 2.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0001654; P:eye development; IMP:ZFIN.
DR GO; GO:1905812; P:regulation of motor neuron axon guidance; IMP:ZFIN.
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; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 1: Evidence at protein level;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119,
KW ECO:0000313|RefSeq:XP_005171292.1};
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 Proteomics identification {ECO:0007829|PeptideAtlas:A0A8M2BIM9};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
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..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..1259
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035479334"
FT DOMAIN 34..222
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 222..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1036..1060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..340
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..427
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..472
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..513
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..563
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..613
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..660
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..676
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..795
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..828
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..859
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..955
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 956..967
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..979
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1050
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1060
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1259 AA; 129118 MW; FDC213053147972B CRC64;
MKFRLLSWLV GAHLALGYLS SALHVMEERG SKGHLILTDL VGMPLPPSVS FITGYEGYPA
YSFGPHANVG RLTQSFVPEP FFTDFAIIVT VKPSSSRGGV LFAITDPSQT IVQLGLALTP
VEDQTQRIVL YYSEPRSANS AEVASFKVPD MTQQWSRFTL SVERQEVRLY MDCDEYHIAP
FKRSQQPLSF KPGSGIFVAN AGSTGLERFV GSIQQLVIKP DPRAAEEQCE EDDPSLQASG
DRSGDGDYDD EEEHARREET FGQTNNKEKT LRPTSPVEAP PIQSPDIEEG GFSGHVTPID
ERLLRGTYKT DETGERVGQK GERGEPGPAG PPGPPGPPGT SVPIRHSGQP GPRGPQGPIG
QPGGRGRPGK DGQPGSKGED GKPGQRGQTG PPGLPGESGV KGEKGDPGVG RTGLPGPPGP
PGPPGPSKPV KVPYGFDALG SGFGDADIDT ELLRGPPGPP GPPGIPGPPG PNSPLGGLLP
GPPGAPGKDG RDGQSGLPGV PGQDGLPGQQ GPKGAKGEHG IRGPPGPKGE NGDPGQRGPP
GPFGTMGPRG LPGPPGPPGP PGPINNNFMV DTLKDFEGSG ESGSFLGTGI LKGYQGPPGL
PGPPGPQGPP GANGPPGLSV KGERGSPGPD GIHGLAGLPG ARGPKGDKGN PGEKGERGRD
GLNITGPPGP PGPPGPIINF QDLFLNDTAA KLNLTKIRGL PGPMGPEGLP GRAGFPGPRG
PKGEIGFPGV QGPPGLKGDK GEPGVSIAAD GSIITSLRGP RGPKGTKGDI GLAGPHGIPG
PIGPPGLKGG YGIPGRPGRP GIAGRKGDKG DASGPSGPPG PPGPPGPPGR VIGLNGTVFP
VPPRPHCKTP VNNNNSQQGV KGEKGDEGNP GLSGTPVPHA YVGPKGDNGY NGQKGEKGDP
GLPGPPGLPG RTGLVGPKGE SIVGPPGDTG APGPPGLPGY GSPGPQGPPG APGPPGTSSL
YSSAASLPGP PGPPGPPGAP GYGNPVSTYK NSQTLMRESS QAAEGTMGYV IDKSELYIRV
RGGWKKIELG ELIPVPEDSS SSALSQGLSR PSDRSVPRVH SQELKSFLPG YNLLPDTTHS
MPALHLVALN APFSGDMHGI RGADYQCYQQ ARARGLTSTY RAFLSSHLQD LSTIVKKADR
FNLPVVNLKG EVLFSSWMAM FSGNGGVFDP LTPIYSFDGR NVLTDQAWSQ KLVWHGSSTV
GIRMTTNYCE AWRTGDMAVT GQASLLQTGR LLGQHTRSCS NHFIILCIEN SYIQHPGRN
//
