ID A0A6J2J688_9PASS Unreviewed; 1342 AA.
AC A0A6J2J688;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 28-JAN-2026, entry version 23.
DE SubName: Full=Collagen alpha-1(XVIII) chain isoform X2 {ECO:0000313|RefSeq:XP_027607785.2};
GN Name=COL18A1 {ECO:0000313|RefSeq:XP_027607785.2};
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_027607785.2};
RN [1] {ECO:0000313|RefSeq:XP_027607785.2}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_027607785.2};
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_027607785.2; XM_027751984.2.
DR GeneID; 114004210; -.
DR CTD; 80781; -.
DR Proteomes; UP000504627; Unplaced.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00247; Endostatin-like; 1.
DR CDD; cd00110; LamG; 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; IPR050938; Collagen_Structural_Proteins.
DR InterPro; IPR010515; Collagenase_NC10/endostatin.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR37456:SF5; COLLAGEN TYPE XIII ALPHA 1 CHAIN; 1.
DR PANTHER; PTHR37456; SI:CH211-266K2.1; 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; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119,
KW ECO:0000313|RefSeq:XP_027607785.2};
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 Reference proteome {ECO:0000313|Proteomes:UP000504627};
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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1342
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030157389"
FT DOMAIN 32..220
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 219..1025
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..236
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..284
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..454
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..494
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..534
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..586
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..606
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..710
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..803
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..852
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..925
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..971
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..995
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1005..1017
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1342 AA; 137393 MW; 831C99B73B1C7E50 CRC64;
MRPGCPPPRL LLGLFVLLVP ATSQEPENLS AEVSLLELIG DPPPEEILKI YGPDNNPGYV
FGPNANTGQV ARYHLPSPFY RDFSLLFHIQ PTTPWAGVLF AITDSSQSII YVGVKLSELR
AGKQQIIFYY TEPGSPSSYP AATFTVPTLL NQWTRFAISV EEDEVILYLD CEEHERVRFE
RSPDEMELED GSGLFVAQAG GADPDKYQGV IADLKLRGDP RAAERQCEEE EDDTELSGDF
GSGAEGGHQP SGKVGGVPGL VDAVPVTSPP VAGGSGPRSS GGSPQQAERT RAEETLRVSM
GGTGPKGEKG EKGERGLKGD SGTGGIMGTS SVKGQKGEKG DLGIKGSAGF GYPGSKGQKG
EPGDPGPPGT LSRHTDGSVV EQVTGPPGPP GKDGAPGRDG EPGDPGEDGK PGDMGPQGFP
GMPGEPGLKG EKGDPGVGPR GPPGPPGPPG PPGPSSKNDK LTFIDMEGSG FGGDLESLRG
PRGPPGPPGP PGVPGLPGEP GRFGMNRTDL PGPPGLPGRD GIPGPPGPAG PQGPPGRDGE
AGQPGPKGER GDVGDLGLPG VPGPKGNKGE MGPAGPPGEM GLAGLPGPIG PRGQPGPPGP
PGPPGPGYEA GFGDMEGSGL SFTPGPPGPE GPQGLPGLPG AKGEVGSPGQ PGLPGPKGDA
GMPGVDGRPG LEGFPGPQGP KGDQGNPGEK GERGQDGVGL PGPPGPPGPP GQVITLSSED
KSLVAFPGPE GRPGHAGFPG PVGPKGDQGS TGPQGSPGLK GEKGEPGVII SPDGTVVTAK
VKGEKGEPGL QGPMGPSGPQ GQAGMKGEIG FPGRPGRPGM NGLKGEKGDP ADVLGLRGPP
GPPGPPGPPG PPGSIAYNSG NTFSDSSHPA LPAFPGLHQF PGQKGEKGDA GPPGPPGHFP
YDPTHFGTNL RGDKGDAGPK GEKGEPGSTP LYNPSVSRLP GPPGPQGYPG LPGPKGDSIV
GPPGPPGPQG PPGIGYEGRQ GPPGPPGPPG PPSFPGPHRQ AISIPGPPGP PGPPGPPGTS
GLSLGLRAMP TYQLMLSTAH ELPEGSLIFL TDRQELYVRL RGGFRRVLLE EHNLIPSSAL
DNEVYDKPPT LHYAGTQPHG PLHPLRNHVP PPTARPWRGD EVVANQHRLP EQPLLHHQDE
LLNSYYIHRR PDPAPVAAHV HQDFQPALHL VALNTPLSGG MRGIRGADFQ CFQQARQVGL
AGTFRAFLSS RLQDLYSIVR RADRAAVPIV NLRDEVLFNN WEALFTGSGA PLRAGTRILS
FDGRDVLRDA GWPQKSVWHG SDAKGRRLPD SYCETWRTEE RAITGQASSL TSRKLLEQVA
SSCQHAFIVL CIENSFMTAA KK
//
