ID A0A8J1LUA9_XENLA Unreviewed; 934 AA.
AC A0A8J1LUA9;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE SubName: Full=Collagen alpha-1(XV) chain-like isoform X1 {ECO:0000313|RefSeq:XP_041432626.1};
GN Name=LOC121398112 {ECO:0000313|RefSeq:XP_041432626.1};
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_041432626.1};
RN [1] {ECO:0000313|RefSeq:XP_041432626.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_041432626.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_041432626.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
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DR RefSeq; XP_041432626.1; XM_041576692.1.
DR AlphaFoldDB; A0A8J1LUA9; -.
DR GeneID; 121398112; -.
DR KEGG; xla:121398112; -.
DR CTD; 121398112; -.
DR OrthoDB; 10060752at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR GO; GO:0005604; C:basement membrane; IBA:GO_Central.
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; IBA:GO_Central.
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};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..934
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035185177"
FT DOMAIN 678..722
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 762..928
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 37..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..65
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..313
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..357
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..405
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..450
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..595
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..621
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..634
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 934 AA; 98520 MW; F27E304EBF666D6D CRC64;
MERMGCRTLL IVALITMNHL LPAQAQWLIF GDRDKEKEIS APKPTSPSPT SKQSENELDD
LDEESESIKL TPPPMMPHST IHPEEKKELF HQTEPPIIII PEETTTPVKP TTTAMKKTTG
MTQGPTTLKE ATVSTAGNIK IRESEKPAKE FHETPRYFSE PREPPALQPE LQTTVPAAAR
ETTQLQSTTS HQYPLTEGQG FAELIPSTTT LLPDIHKAKS EEDFSPEESI VGKQDIEPVE
ITPRSPYRFP DIDPEKLNLS GCTCPAIPGP PGLKGDRGDP GPPGLPGSPG HTGERGYMGM
PGPPGPQGPP GPQGIPGQPG TVGIFKAKES ENEVVLDRPG PPGPEGQRGP PGLQGHPGPQ
GPEGPEGPQG PPGLPGLPGV PGHPGLIGPK GDQGPEGLPG LRGPPGQSGF QGYEGLQGSE
GLRGPEGPPG PQGLPGIEGP QGLPGPEGSP GIAGLPGLPG MDGSPGLSGH QGPEGAPGIQ
GLIGQKGEKG DTGASGLPGI QGLHGQKGEP GPQGPPGPAS EGLCCKGEIV PSIPAVVPGP
QGPKGEKGDP GEGCANHCSH TLSNDISPHG PPGPQGPPGP PGPPGLPGPP GPPQTNLPSR
FQEDGRSDVY GSLLYSGLPG SPGSPGPPGP PGPPGVVYIN RVYPVPPRPH CKQTVPIESK
TTRSDSAAEP QKYLKSWVFQ TKDEMSQAWE EVTEGALVYV KDQSAAYFRS SVGWSKILLE
DIDPILSADD PLVQEEYAEE DPESTNEHVS VPQSISYRIP SLRLVALNVP MSGGMSGIRG
ADLQCYNQAQ EMSLYGTFRA VLTSSSQSLS SIVKRTDQNL PIVNIRGDLL MMSWNSLFEN
KSKPFKSNAP VYSFNGRDLL TDTLWPQKAF WHGSSQKGNS IRNRNCREWR SSSVAEGLGS
PLTGKWIQDS DSYECSKPLA VLCIEIAFPY QHMW
//
