ID A0A8J6GX05_MICOH Unreviewed; 1788 AA.
AC A0A8J6GX05;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 1.
DT 28-JAN-2026, entry version 16.
DE SubName: Full=Collagen alpha-1(XVIII) chain {ECO:0000313|EMBL:KAH0518087.1};
GN ORFNames=LTLLF_116980 {ECO:0000313|EMBL:KAH0518087.1};
OS Microtus ochrogaster (Prairie vole).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Arvicolinae; Microtus.
OX NCBI_TaxID=79684 {ECO:0000313|EMBL:KAH0518087.1, ECO:0000313|Proteomes:UP000710432};
RN [1] {ECO:0000313|EMBL:KAH0518087.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LTLLF {ECO:0000313|EMBL:KAH0518087.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAH0518087.1};
RA Glass D.;
RT "Studies in the Genomics of Life Span.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00090}.
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:KAH0518087.1}.
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DR EMBL; JAATJU010012500; KAH0518087.1; -; Genomic_DNA.
DR Proteomes; UP000710432; 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:0001525; P:angiogenesis; IEA:TreeGrafter.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0001886; P:endothelial cell morphogenesis; IEA:TreeGrafter.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
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; 2.
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; -; 2.
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; IPR010363; DUF959_COL18_N.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1034; COLLAGEN ALPHA-1(XVIII) CHAIN; 1.
DR Pfam; PF01391; Collagen; 2.
DR Pfam; PF20010; Collagen_trimer; 2.
DR Pfam; PF06121; DUF959; 1.
DR Pfam; PF06482; Endostatin; 1.
DR Pfam; PF13385; Laminin_G_3; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF63501; Frizzled cysteine-rich domain; 1.
DR PROSITE; PS50038; FZ; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119, ECO:0000313|EMBL:KAH0518087.1};
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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1788
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035305203"
FT DOMAIN 228..279
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT REGION 48..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1077..1100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1302..1376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..237
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..611
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..651
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..679
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..698
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..758
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..834
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..868
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1014
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1345..1356
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1788 AA; 190989 MW; E0595FD632C02271 CRC64;
MAPDPSRRLW LLLLLLSCCP EPARPDNNPL NPLNSLRPLV WLWSTKTDDP VSKPQISSPV
QSTGSPTTHV VPQDGLTDQQ TTPADSRLPL QDREAGQNGT PTAPALPIPP TASAASPDMK
EENVAGVGAK ILNVAQGIRS FVQLWDEDTA TQNSAGTETS ASTIPTVLLT PTEFSSTPQE
GETTLWQSGG IPSSPDVQTT KAGTLAVPTQ PPPSLNSLQA PLRRPPGPPT PPGPPPALPP
CRQFCEVLED GCWKHLDEGR LPVKCASLPS QEDGYCVFIG PAAENIAEEV GLPQLLGDPL
PQQIQQIEDP DVGPAYIFGP DSSGGQVAQH HFPRLFFRDF SILFHIQPAT KAAGVLFAIT
DAAQTVVSLG VKLSGVQDGY QNISLLYTEH GASQTRKGAS FHLPAFVGQW THFALSVDGR
SVALYIDCEE FQKVPFARSP QGLELEHDSG LFVGQAGAAD PDKFQGKISE LKIRQNPRVS
PVHCLDEEDD DEDRASGDFG SGFEESSKPH REEVFRAYLA QLVPRVLQAQ WYRTPVHNLS
LEHKDPQGLR GHQEKMELQE GTVNRVTLVK MEGRVTLGLK AFQEPQEKWA PRGDPGVGVR
GPPGPPGPPG PSFRQDKLTF IDMEGSGFSG DMESLRGPRG FPGPPGPPGV PGLPGEPGSF
GVNSSYAPGP AGLPGVPGKE GPPGFPGPPG PPGPPGKEGP PGVAGQKGSS HGDFVLLSVQ
GSKGDLGPVG VPGKTGMAGP PGPTGPPGPP GPPGPPGPGF AAGFDDMEGS GMPFWPTARS
SDGLQVLPVG RSRRRVPGQA DSGPSICLSQ GEAGADGIQG IPGLPGREGA AGPRGPKGEK
GTQGEKGNPG KDGVGLPGLP GPPGPPGPVV YVSNEDSSVS PKLTVPFFPQ GKPGYAGFPG
PAGPKGDLGS KGEQGLPGPK GEKGEPGAIF GPDGRALGPA QKGAKGEPGF RGPPGPYGRP
GHKGEIGFPG RPGRPGTNGL KGEKGEPGDA SLGFSMRGLP GPPGPPGPPG PPGMPIYDSN
VSGQSFILRG FSPIAASGIL SGYLWNGSVG RLWSLADLDY QDSKVRSLGI TVHAQVWGSG
VPGPSGPKGD KGEVGPPGPP GQFPIDFFHL GAEMKITTST CRVTRETEGT LDRKESGENL
GLLVVDSSAQ VCLDHLAHLD TLEFRVQRER AFGAHLALLA LRDLLVLAMR GVRDRQDRQD
RQDLPRSLVL IGRQVRIWAT YQTMLDKVRE VPEGWLIFVA EREELYVRVR NGFRKVLGNE
VAVLPPLVQL HEGSPYTRRE HSYSTARPWR ADDILVNPPR LPDPKPYPGV PHHHSAYVHQ
PPARPTSPPA HTHQDFQPVA FVESGRPGLP GQQGVPGPSG PKGDKGEVGP PGPPGQFPID
FFHLGAEMKI TTSTCRVTRE TEGTLDRKES GENLGLLVVD SSAQVCLDHL AHLDTLEFRV
QRERAFGAHL ALLALRDLLV LAMRGVRDRQ DRQDRQDLPR SLVLIGRQVR IWATYQTMLD
KVREVPEGWL IFVAEREELY VRVRNGFRKV LGNEVAVLPP LVQLHEGSPY TRREHSYSTA
RPWRADDILV NPPRLPDPKP YPGVPHHHSA YVHQPPARPT SPPAHTHQDF QPVLHLVALN
SPLSGGMRGI RGADFQCFQQ ARAVGLAGTF RAFLSSRLQD LYSIVRRADR GTVPIVNLKD
EVLSASWDAL FSGSQGQLQP GARIFSFDGR DVLRHPAWPQ KSIWHGSDPS GRRLMENYCE
TWRTEASEAT GQASSLLSGR LLEQRAASCH NAYIVLCIEN SFMTSFSK
//
