ID A0A6J2IRA7_9PASS Unreviewed; 846 AA.
AC A0A6J2IRA7;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 28-JAN-2026, entry version 22.
DE SubName: Full=Collagen alpha-1(XVIII) chain-like isoform X2 {ECO:0000313|RefSeq:XP_027602367.1};
GN Name=LOC114001427 {ECO:0000313|RefSeq:XP_027602367.1};
OS Pipra filicauda (Wire-tailed manakin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Pipridae; Pipra.
OX NCBI_TaxID=649802 {ECO:0000313|Proteomes:UP000504627, ECO:0000313|RefSeq:XP_027602367.1};
RN [1] {ECO:0000313|RefSeq:XP_027602367.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_027602367.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
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DR RefSeq; XP_027602367.1; XM_027746566.2.
DR AlphaFoldDB; A0A6J2IRA7; -.
DR GeneID; 114001427; -.
DR Proteomes; UP000504627; Unplaced.
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; 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:SF1114; COLLAGEN ALPHA-1(XVIII) 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:UP000504627}.
FT DOMAIN 567..610
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 675..840
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 54..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..188
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..224
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..240
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..288
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..318
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..333
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..361
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..405
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..418
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..560
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..646
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 846 AA; 87318 MW; 4D5681B069B2F63E CRC64;
MSQGPPSWAA AGPRGSTMGS GSAWGLLRTL CILLVLAGRL CPATAQWFYL GSEDTTLDPG
TSLTTPTLDG EEDAETSMEP TGKVLLSKPP LAKVPRRRDH LTRGTAKGPG HAPPRTRGQQ
HRPTATPEIF EGSAVEEEFL QIQTTTKGLP RGVPPAPEMD PALQVHNGSD CVCPVHPGPP
GRAGPPGPKG EKGDRGFPGE RGQPGISGDR GKSGSPGQPG HQGPRGPPGP PGPPGPPGPP
GTWGARSLPA PAALPEGLEN ELGPSSPVGN PGPPGPPGLP GMPGPPGYPG HDGPPGVPGR
EGKPGPPGPP GAVGPPGFPG AEGTPGSPGS AGPDGPPGAP GLPGPQGPPG VPGHEGPPGP
TGPASLPGKP GLRGEPGFPG LKGEKGEYGL PGMPGSPGRT GETGPPGMPG PMGPPGPPGD
YRCDLRHGGH RGLAGAPGPK GEKGDPGEPG CCYREQGCKP GHLPFPSTGS QPSSWGSIRG
YQTDSKEEPE IYGAIIPHGV RGPPGPPGPP GPPGPPGLLY LNRVYPVRAQ PPCKQPVAPD
PGWAADADTR QTEPSDCRTD PRRQTWVFRS KELMVKASGA VPEGSLVYVQ EGSSAFLRTP
AGWSRLLLED SRSVLAGDDP SASTPRYQEA KRVQTRGPNT VSPVQSPMDS LVQKEEGQGL
PKIPPTTIAP RIPSLRLAAL NVPLSGDMRG IRGADLQCYR QSQEAGLYGT FRAFLSAPTQ
DLVSIVKRTD RTLPIVNLKG QLLAKSWSSL FEGQPGATPR GPIYSFNGRN ILTDPLWPHR
LAWHGSTVRG GHARRWDCQG WRGSSMAEGM ATPLGQGRLL AGHRHNCSTP LAVLCVEVAF
PYRHMW
//
