ID A0A2Y9G785_NEOSC Unreviewed; 1301 AA.
AC A0A2Y9G785;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 28-JAN-2026, entry version 33.
DE SubName: Full=Collagen alpha-1(XVIII) chain isoform X3 {ECO:0000313|RefSeq:XP_021534901.1};
GN Name=COL18A1 {ECO:0000313|RefSeq:XP_021534901.1};
OS Neomonachus schauinslandi (Hawaiian monk seal) (Monachus schauinslandi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC Monachinae; Monachini; Neomonachus.
OX NCBI_TaxID=29088 {ECO:0000313|Proteomes:UP000248481, ECO:0000313|RefSeq:XP_021534901.1};
RN [1] {ECO:0000313|RefSeq:XP_021534901.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_021534901.1};
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_021534901.1; XM_021679226.2.
DR GeneID; 110571100; -.
DR CTD; 80781; -.
DR Proteomes; UP000248481; Chromosome 1.
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 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; 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; 1.
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_021534901.1};
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:UP000248481};
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..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..1301
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015893863"
FT DOMAIN 41..229
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 90..228
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 231..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..282
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..358
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..422
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..462
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..490
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..506
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..516
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..551
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..571
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..660
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..677
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..819
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..892
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 904..916
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..962
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..984
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1301 AA; 132471 MW; DDDAF59450E9C33E CRC64;
MAPRWPWLRP RPRSLLDVLA PLVLLLGVRA ASAEPESLGT EVGLLQLLGE PPPPQVTQVD
DPDIGPAFVF GPDANSGQVA RYHFPSPFFR DFSLHFHVRP ATEDAGVLFA ITDAAQAVVS
VGVRLSGVRD GHQHIQLLYT EPGATRTHTA ASFRLPAFTG QWTRFALSVD GATVALFVDC
ELFQRVPLVR SLRGLELEPG AGLFVAQAGG ADPDKFQGMI AELRVRGDPH VSPLHCLEED
DEDSGGVSGD FGSGLEETRE PLREQSGPSP KPSLPEAPPV TSPPLAAGRD VEDSRTEEIE
EETTVSSLGA RTLPGLDAVT IESVRSPGGG LEEGPAVQSP NARPIPGPQG PPGPPGPPGK
DGAPGRDGEP GDPGEDGRPG DPGPQGFPGT PGDAGPKGEK GDPGVGPRGP PGPQGPPGPP
GPSFRHDKLT FIDMEGSGFG GDLESLRGPR GFPGPPGPPG VPGLPGEPGR FGMNSSDVPG
PAGLPGVPGR DGPPGLPGTP GPPGPPGKDG GPGKMGQKGS PGEVGAPGPK GRQGDSGPVG
APGENGLAGA PGPAGPPGPP GPPGPPGPPG PGLAAGFDDM EGSGRPFWST AQGASGSQGP
PGPPGVKGDP GITGPPGAKG EVGADGPPGF PGLPGREGSA GAQGPKGEKG TQGEKGDPGR
DGVGQPGLPG PPGPPGPVVY MSEQDRVLGG VPGPEGRPGF AGFPGPAGPK GDLGSKGQRG
LPGPKGEKGE PGPVFSPDGS LLAPAQKGAK GEPGFRGPPG PYGRPGHKGE IGFPGRPGRP
GMNGLKGEKG EPGHSSVGFG LRGPPGPPGP PGPPGPPGTP IYDSNAFMES GRPGPPGLPG
LQGPSGPKGD KGDVGPPGPP GQFPFDLLQL GTEMKGEKGD RGDTGQKGER GEPGGGGFFG
SSVPGPPGPP GYPGIPGPKG ESIRGQPGPP GPQGPPGIGH EGRQGPPGPP GPPGPPGPPS
FPGPYRQTIS VPGPPGPPGP PGPPGTMGTS SGQVRIWATY QTMLDKVPEV PEGWLIFVAE
REELYVRVRN GLRKVLLEAR TPLPHGTDNE VAALQPPVGN PYPRRELTHS TARPWRADDI
LANPPRLLDP QPYPGAPQHG SYLHFQPARP TGRPTHTHTH QDYHPVLHLV ALNSPQPGGM
RGIRGADFQC FQQARAVGLA GTFRAFLSSR LQDLYSVVRR ADRTSVPIVN LRDEVLFPSW
EALFSGSEGQ LKPGARIFSF DGRDVLQHPA WPQKSVWHGS DPSGRRLTDS YCETWRTEAA
AATGQASSLL AGRLLAQKAA SCHSAFIVLC IENSFMTSFS K
//
