ID A0A151NAH2_ALLMI Unreviewed; 1387 AA.
AC A0A151NAH2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 28-JAN-2026, entry version 34.
DE SubName: Full=Collagen alpha-1(XVIII) chain isoform A {ECO:0000313|EMBL:KYO33599.1};
GN Name=COL18A1 {ECO:0000313|EMBL:KYO33599.1};
GN ORFNames=Y1Q_0008757 {ECO:0000313|EMBL:KYO33599.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO33599.1, ECO:0000313|Proteomes:UP000050525};
RN [1] {ECO:0000313|EMBL:KYO33599.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO33599.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYO33599.1}.
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DR EMBL; AKHW03003682; KYO33599.1; -; Genomic_DNA.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000050525; Unassembled WGS sequence.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; 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:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
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; IPR050149; Collagen_superfamily.
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; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1019; COLLAGEN ALPHA-5(IV) CHAIN ISOFORM X1; 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, ECO:0000313|EMBL:KYO33599.1};
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:UP000050525};
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..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1387
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007585885"
FT DOMAIN 38..226
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 87..225
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 234..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..1059
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..244
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..387
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..480
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..523
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..632
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..667
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..739
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..829
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..881
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 942..959
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..974
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1004
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1028
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1049
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1387 AA; 142088 MW; 9625A35BC8371996 CRC64;
MRGRCPQRRR RPRPQLLPGL FVLLAAAASQ ERENFSTEVG 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
LPGKDGEPGD PGEDGKPGDT GPQGFPGTPG EPGLKGEKGD PGVSVKGSPG PPGPPGPPGI
PGLSSKQDKL TFIDMEGSGF AGDLESLRGP RGPPGPPGPP GVPGLPGEPG RFGMNHTAIP
GPPGLPGKDG SPGLQGPSGP PGPPGREGLP GQPGFRGEKG DSGDLGLPGA PGPKGSKGET
GPQGSPGETG LAGLPGPIGP RGQPGPPGPP GPGYEAGFGD MEGSGIPIVS SVPGPRGPEG
PQGPPGLPGL KGDIGSLGQP GVPGQKGDPG TPGTNGQPGL EGFPGPQGPK GDQGSPGVKG
ERGQDGVGLP GPPGPPGPPG EIVYASNKTL AVLPGPEGRP GHAGFPGPVG PKGEAGSPGL
QGFPGLKGEK GEPGVIIGPD GTVTALDTKG EKGEPGLRGP VGPLGPHGRP GQKGEIGFPG
RPGRPGMNGL KGEKGDPADP SGGFSVPGLP GPPGPPGPPG SPGSIVPIYD GNAFTESGPP
GPPGLPGYQG VPGHKGEKGD TGAPGPPGQF PYDLSRFGAA FRGEKGEQGD SGLKGEKGEP
GGGTLYGPGV GQPGLPGPQG YPGLPGPKGD SIVGPPGPPG PQGPPGIGYE GRQGPPGPPG
PPGPPSFPGP HRQTNVVGPP GPPGPPGPPG TSGTSASSGL KILPSYQAML STAHEVPEGW
LVFIVDREEL YVRVRNGFRR ILLEDHTVIS STALDNEVYD KPPSIHFARG SSPSSGSQPH
VPVHPHRDYN TYATVRPWGG DDIIANHHRL PKQPSIHQGA QHQQENLHDF YPNRRPEDTP
SAMHTHHDFQ PALHLVALNT PLSGSMRGIR GADFQCFQQA REVGLTGTFR AFLSSRLQDL
YSIVRRADRS SVPIVNLRDE VLFNNWESLF SGTEAQLRAA THILSFNGKD ILRDSTWPQK
SVWHGSDSKG RRLTENYCET WRTDSSVVTG QASSLSSGKL LEQKASSCQN AFIVLCIENS
FMTSSKK
//
