ID   A0A8J1LSV6_XENLA        Unreviewed;       860 AA.
AC   A0A8J1LSV6;
DT   25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 1.
DT   28-JAN-2026, entry version 18.
DE   SubName: Full=Collagen alpha-1(XV) chain-like isoform X2 {ECO:0000313|RefSeq:XP_041432627.1};
GN   Name=LOC121398112 {ECO:0000313|RefSeq:XP_041432627.1};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_041432627.1};
RN   [1] {ECO:0000313|RefSeq:XP_041432627.1}
RP   IDENTIFICATION.
RC   STRAIN=J_2021 {ECO:0000313|RefSeq:XP_041432627.1};
RC   TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_041432627.1};
RG   RefSeq;
RL   Submitted (AUG-2025) to UniProtKB.
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DR   RefSeq; XP_041432627.1; XM_041576693.1.
DR   AlphaFoldDB; A0A8J1LSV6; -.
DR   GeneID; 121398112; -.
DR   CTD; 121398112; -.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   GO; GO:0005594; C:collagen type IX trimer; 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:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR   Gene3D; 3.40.1620.70; -; 1.
DR   Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 2.
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; IPR016187; CTDL_fold.
DR   InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24023:SF1099; COLLAGEN ALPHA-1(XV) CHAIN; 1.
DR   Pfam; PF01391; Collagen; 3.
DR   Pfam; PF20010; Collagen_trimer; 1.
DR   Pfam; PF06482; Endostatin; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
PE   4: Predicted;
KW   Collagen {ECO:0000256|ARBA:ARBA00023119};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186698}.
FT   DOMAIN          604..648
FT                   /note="Collagen type XV/XVIII trimerization"
FT                   /evidence="ECO:0000259|Pfam:PF20010"
FT   DOMAIN          688..854
FT                   /note="Collagenase NC10/endostatin"
FT                   /evidence="ECO:0000259|Pfam:PF06482"
FT   REGION          30..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          189..561
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..45
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..239
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        271..283
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        309..331
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        360..376
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        495..521
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        535..547
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        548..560
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   860 AA;  90248 MW;  A8A6C722726A0DD3 CRC64;
     MMPHSTIHPE EKKELFHQTE PPIIIIPEET TTPVKPTTTA MKKTTGMTQG PTTLKEATVS
     TAGNIKIRES EKPAKEFHET PRYFSEPREP PALQPELQTT VPAAARETTQ LQSTTSHQYP
     LTEGQGFAEL IPSTTTLLPD IHKAKSEEDF SPEESIVGKQ DIEPVEITPR SPYRFPDIDP
     EKLNLSGCTC PAIPGPPGLK GDRGDPGPPG LPGSPGHTGE RGYMGMPGPP GPQGPPGPQG
     IPGQPGTVGI FKAKESENEV VLDRPGPPGP EGQRGPPGLQ GHPGPQGPEG PEGPQGPPGL
     PGLPGVPGHP GLIGPKGDQG PEGLPGLRGP PGQSGFQGYE GLQGSEGLRG PEGPPGPQGL
     PGIEGPQGLP GPEGSPGIAG LPGLPGMDGS PGLSGHQGPE GAPGIQGLIG QKGEKGDTGA
     SGLPGIQGLH GQKGEPGPQG PPGPASEGLC CKGEIVPSIP AVVPGPQGPK GEKGDPGEGC
     ANHCSHTLSN DISPHGPPGP QGPPGPPGPP GLPGPPGPPQ TNLPSRFQED GRSDVYGSLL
     YSGLPGSPGS PGPPGPPGPP GVVYINRVYP VPPRPHCKQT VPIESKTTRS DSAAEPQKYL
     KSWVFQTKDE MSQAWEEVTE GALVYVKDQS AAYFRSSVGW SKILLEDIDP ILSADDPLVQ
     EEYAEEDPES TNEHVSVPQS ISYRIPSLRL VALNVPMSGG MSGIRGADLQ CYNQAQEMSL
     YGTFRAVLTS SSQSLSSIVK RTDQNLPIVN IRGDLLMMSW NSLFENKSKP FKSNAPVYSF
     NGRDLLTDTL WPQKAFWHGS SQKGNSIRNR NCREWRSSSV AEGLGSPLTG KWIQDSDSYE
     CSKPLAVLCI EIAFPYQHMW
//