ID A0A8M3APP4_DANRE Unreviewed; 1315 AA.
AC A0A8M3APP4;
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 X1 {ECO:0000313|RefSeq:XP_009296788.1};
GN Name=col15a1b {ECO:0000313|RefSeq:XP_009296788.1,
GN ECO:0000313|ZFIN:ZDB-GENE-070912-689};
GN Synonyms=cb491 {ECO:0000313|RefSeq:XP_009296788.1}, sb:cb491
GN {ECO:0000313|RefSeq:XP_009296788.1}, si:dkeyp-93c5.1
GN {ECO:0000313|RefSeq:XP_009296788.1}, wu:fb50f05
GN {ECO:0000313|RefSeq:XP_009296788.1}, wu:fc22d09
GN {ECO:0000313|RefSeq:XP_009296788.1};
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_009296788.1};
RN [1] {ECO:0000313|RefSeq:XP_009296788.1}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:XP_009296788.1};
RC TISSUE=Fibroblasts and whole tissue
RC {ECO:0000313|RefSeq:XP_009296788.1};
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_009296788.1; XM_009298513.5.
DR AlphaFoldDB; A0A8M3APP4; -.
DR FunCoup; A0A8M3APP4; 126.
DR GlyGen; A0A8M3APP4; 2 sites.
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: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:0001654; P:eye development; IMP:ZFIN.
DR GO; GO:1905812; P:regulation of motor neuron axon guidance; IMP:ZFIN.
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; 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_009296788.1};
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:A0A8M3APP4};
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..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1315
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035420173"
FT DOMAIN 90..278
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 32..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..1045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1092..1116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..47
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..396
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..483
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..528
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..569
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..619
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..669
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..716
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..732
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..851
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..884
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..915
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1001..1011
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1023
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1035
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1106
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1315 AA; 134956 MW; D9B97DE17332C79F CRC64;
MAPLTSLLLL SLVSLSGQIQ WFRFLWVPET SSPAPAVSTP ADTSSTEAAE ENTEHVLPTS
PPAPTAAPAD TARAKRPLKR WKSERGSKGH LILTDLVGMP LPPSVSFITG YEGYPAYSFG
PHANVGRLTQ SFVPEPFFTD FAIIVTVKPS SSRGGVLFAI TDPSQTIVQL GLALTPVEDQ
TQRIVLYYSE PRSANSAEVA SFKVPDMTQQ WSRFTLSVER QEVRLYMDCD EYHIAPFKRS
QQPLSFKPGS GIFVANAGST GLERFVGSIQ QLVIKPDPRA AEEQCEEDDP SLQASGDRSG
DGDYDDEEEH ARREETFGQT NNKEKTLRPT SPVEAPPIQS PDIEEGGFSG HVTPIDERLL
RGTYKTDETG ERVGQKGERG EPGPAGPPGP PGPPGTSVPI RHSGQPGPRG PQGPIGQPGG
RGRPGKDGQP GSKGEDGKPG QRGQTGPPGL PGESGVKGEK GDPGVGRTGL PGPPGPPGPP
GPSKPVKVPY GFDALGSGFG DADIDTELLR GPPGPPGPPG IPGPPGPNSP LGGLLPGPPG
APGKDGRDGQ SGLPGVPGQD GLPGQQGPKG AKGEHGIRGP PGPKGENGDP GQRGPPGPFG
TMGPRGLPGP PGPPGPPGPI NNNFMVDTLK DFEGSGESGS FLGTGILKGY QGPPGLPGPP
GPQGPPGANG PPGLSVKGER GSPGPDGIHG LAGLPGARGP KGDKGNPGEK GERGRDGLNI
TGPPGPPGPP GPIINFQDLF LNDTAAKLNL TKIRGLPGPM GPEGLPGRAG FPGPRGPKGE
IGFPGVQGPP GLKGDKGEPG VSIAADGSII TSLRGPRGPK GTKGDIGLAG PHGIPGPIGP
PGLKGGYGIP GRPGRPGIAG RKGDKGDASG PSGPPGPPGP PGPPGRVIGL NGTVFPVPPR
PHCKTPVNNN NSQQGVKGEK GDEGNPGLSG TPVPHAYVGP KGDNGYNGQK GEKGDPGLPG
PPGLPGRTGL VGPKGESIVG PPGDTGAPGP PGLPGYGSPG PQGPPGAPGP PGTSSLYSSA
ASLPGPPGPP GPPGAPGYGN PVSTYKNSQT LMRESSQAAE GTMGYVIDKS ELYIRVRGGW
KKIELGELIP VPEDSSSSAL SQGLSRPSDR SVPRVHSQEL KSFLPGYNLL PDTTHSMPAL
HLVALNAPFS GDMHGIRGAD YQCYQQARAR GLTSTYRAFL SSHLQDLSTI VKKADRFNLP
VVNLKGEVLF SSWMAMFSGN GGVFDPLTPI YSFDGRNVLT DQAWSQKLVW HGSSTVGIRM
TTNYCEAWRT GDMAVTGQAS LLQTGRLLGQ HTRSCSNHFI ILCIENSYIQ HPGRN
//
