ID A0A3Q0GEY2_ALLSI Unreviewed; 1368 AA.
AC A0A3Q0GEY2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 28-JAN-2026, entry version 28.
DE SubName: Full=Collagen alpha-1(XVIII) chain isoform X4 {ECO:0000313|RefSeq:XP_025058017.1};
GN Name=COL18A1 {ECO:0000313|RefSeq:XP_025058017.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_025058017.1};
RN [1] {ECO:0000313|RefSeq:XP_025058017.1}
RP IDENTIFICATION.
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_025058017.1; XM_025202232.1.
DR GeneID; 102378688; -.
DR CTD; 80781; -.
DR Proteomes; UP000189705; 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:SF6; COLLAGEN ALPHA-1(XXIII) CHAIN-LIKE ISOFORM X2; 1.
DR PANTHER; PTHR37456; SI:CH211-266K2.1; 1.
DR Pfam; PF01391; Collagen; 4.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SMART; SM00282; LamG; 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_025058017.1};
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 Reference proteome {ECO:0000313|Proteomes:UP000189705};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 18..206
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 67..205
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 214..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 790..1040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..224
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..367
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..417
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..460
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..503
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..544
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..612
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..647
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..719
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..809
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..861
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..939
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..952
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..985
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1009
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1030
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1368 AA; 139785 MW; 3C39AE0FC352D89B CRC64;
MLILNQAGVI IKENFSTEVG LLQLIGDPPP EQITKIYGPD NNPGYVFGPD ANTGQVARYH
LPSPFYRDFS LLFHIQPTTN KAGVLFAITD SSQAVIYIGV KLSDAKEGKQ HIIFYYTEPG
SQSSYAAATF TVSSLLNQWT RFAVSVEDEE VVLFLDCEEY DRIRFERSPD EMELEDGSGL
FVGQAGGADP DKYQGVIADL KIKNDPHAAV LQCEEDEDDT EEMSGDFGSG VEEKLHSSGK
ERGIPTVSGL PKPPPVTSPP IAGRPVEKVS GSSQLQTEHI KAEETPPVST GARVGQKGEK
GEKGERGPKG DSRTGGVPST GGVKGEKGEK GELGVKGSAG FGYPGSKGQK GEPGAPGDPG
PPGPPGPSGT ILQHQDGSVV EHVTGPPGAM GPPGLPGKDG FPGKDGEPGD PGEDGKPGDT
GPQGFPGTPG EPGLKGEKGD PGVSVKGSPG PPGPPGPPGI PGLSSKQDKL TFIDMEGSGF
AGDLESLRGP RGPPGPPGPP GVPGLPGEPG RFGMNHTAIP GPPGLPGKDG SPGLQGPPGP
PGPPGREGLP GQPGFRGEKG DSGDLGLPGA PGPKGSKGET GPQGSPGETG LAGLPGPIGP
RGQPGPPGPP GPGYEAGFGD MEGSGIPIVS SVPGPRGPEG PQGPPGLPGL KGDIGSSGQP
GVPGQKGDPG TPGTNGQPGL EGFPGPQGPK GDQGSPGVKG ERGQDGVGLP GPPGPPGPPG
EIVYASNKTL AVLPGPEGRP GHAGFPGPVG PKGEAGSPGL QGFPGMKGEK GEPGVIIGPD
GTVTALDTKG EKGEPGLRGP VGPLGPHGRP GQKGEIGFPG RPGRPGMNGL KGEKGDPADP
SGGFSLPGLP GPPGPPGPPG SPGSIVPVYD GNAFTESGPP GPPGLPGYQG VPGHKGEKGD
TGAPGPPGQF PYDLSRFGAA FRGEKGEQGD SGLKGEKGEP GGGTLYGPGV VGQPGLPGPQ
GYPGLPGPKG DSIVGPPGPP GPQGPPGIGY EGRQGPPGPP GPPGPPSFPG PHRQTNVVGP
PGPPGPPGPP GTSGTSASSG LKILPSYQAM LSTAHEVPEG WLVFIVDREE LYVRVRNGFR
RILLEDHTVI SSTALDNEVY DKPPSIHFAH GSSPSSGSQP HVPVHPHRDY NTYATVRPWG
GDDIIANHHR LPKQPSIHQG AQHQQENLHD FYPNRRPEDT PSAMHTHHDF QPALHLVALN
TPLSGSMRGI RGADFQCFQQ AREVGLTGTF RAFLSSRLQD LYSIVRRADR SSVPIVNLRD
EVLFNNWESL FSGTEAQLRA GAHILSFNGK DILRDSTWPQ KSVWHGSDSR GRRLTENYCE
TWRTDSSVVT GQASSLSSGK LLEQKASSCQ NAFVVLCIEN SFMTSSKK
//
