ID A0A8B7V6K6_CASCN Unreviewed; 1354 AA.
AC A0A8B7V6K6;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 21.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0000256|ARBA:ARBA00074723};
GN Name=Col15a1 {ECO:0000313|RefSeq:XP_020026987.1};
OS Castor canadensis (American beaver).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Castoridae;
OC Castor.
OX NCBI_TaxID=51338 {ECO:0000313|RefSeq:XP_020026987.1};
RN [1] {ECO:0000313|RefSeq:XP_020026987.1}
RP IDENTIFICATION.
RC TISSUE=Leukocyte {ECO:0000313|RefSeq:XP_020026987.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- FUNCTION: Restin potently inhibits angiogenesis.
CC {ECO:0000256|ARBA:ARBA00058706}.
CC -!- FUNCTION: Structural protein that stabilizes microvessels and muscle
CC cells, both in heart and in skeletal muscle.
CC {ECO:0000256|ARBA:ARBA00058695}.
CC -!- SUBUNIT: Interacts moderately with EFEMP2.
CC {ECO:0000256|ARBA:ARBA00065596}.
CC -!- SUBUNIT: Trimer; disulfide-linked. {ECO:0000256|ARBA:ARBA00061770}.
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_020026987.1; XM_020171398.1.
DR KEGG; ccan:109691419; -.
DR CTD; 1306; -.
DR OrthoDB; 10060752at2759; -.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-ARBA.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
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 FunFam; 3.40.1620.70:FF:000002; Collagen alpha 1 (XV) chain; 1.
DR FunFam; 3.10.100.10:FF:000008; collagen alpha-1(XVIII) chain isoform X1; 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:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR Pfam; PF01391; Collagen; 3.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR Pfam; PF13385; Laminin_G_3; 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_020026987.1};
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..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1354
FT /note="Collagen alpha-1(XV) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034145317"
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 261..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 961..987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1002..1099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..605
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..704
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..752
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1073
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1083..1095
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1354 AA; 139065 MW; 40E67306C72B9D43 CRC64;
MAPRSSARCL RLLLPAISAL LSVVTQARSS AESAFQSHLD LTELIGVPLP SSVSFVTGYG
GFPAYSFGPG ANVGRPARTL IPPTFFRDFA VSAAVKPSSP QGGVLFAITD AFQKVIYLGL
RLAGVEDGHQ KVVFYYTEPG SHVSHEAAVF SVPVMTNRWN RFAVIVQDEE VTLLMDCEEH
SHVLFQRSSR PLTFESSAGI FIGNAGATGL ERFTGSIQQL TIYSNPRTPE ELCEAQESSA
SGEASGLQET DTVAEILEAV TYTQAPPKEP KVEPISTPPT SYFPFEDTEL SGEPVPEGTP
ETNLSIIQHS SPEQGSGEIL NDTLEGVPTE DGDPSTDIGS ADGAFPDSPE EQGTAATTAE
EKMPFTTAQA VEISTVPTGR VTPAMPTQNS GEGTTPGPEN EESLAMTASG EGEVPISSAG
EEEAGTVPTE GPTLSISMST QSLVEEAALG PSSDGFTTAA AMSEVPLNTF EEEEASGAPT
DGLVAFTPTA AFEQAVTSAP IDEVLAAATT EEAGGEGSGG TPPVEPLLPT AMVAPEGRVS
VTQQVHVGMK GQAEPKGEKV GAEAEGSGLD WGLDFGSGFK DLVSREELLR GPPGPPGPPG
PPGSPGIPGT DVFMGPPGSP GEDGAFGEPG LPGPEGQPGL DGASGQPGMK GEKGARGPNG
SVGEKGDPGS RGLPGPPGKN GQAGTPGVMG PPGPPGXPGP PGPGCPTELG YKDIEGSGST
RLLSEPRISG PTASSGLKGE KGDRGPKGER GMDGISTVGP PGPRGPPGRI EVLSSSLINI
THGSKNFSDI PELMGPPGPD GLPGLPGFPG PRGPKGDTGV PGFPGLKGEQ GEKGEPGTIL
TGDIPLEMVK GKKGEPGVHG APGPMGPKGP PGHKGEFGLP GRPGRPGLNG LKGAKGDRGV
MMLGPPGPPG PPGPPGPPGA VVNIKGAIFP VPVRPHCKTP VGTTHPGDPE LITFHGVKGE
KGSWGLPGSK GEKGDQGAQG PPGPPVDPTY LRHFLNNLKV ENGDRGLRGE SNGNFFVSGP
PGLPGNPGLI GQKGEAIVGP QGPPGTPGLP GPPGFGRPGA PGPPGPPGPP GPPAILGAAV
ALPGPPGPPG QPGLPGPRNL VTALSSMDDM LQTAHLIIEG TFIYLRDSAE FFIRVRDGWK
KLQLGELIPL PADSPPPPAL SSNPYQPQPP LNPILSANFE KPALRLVALN MPFSGDIRAD
FQCFQQARAT GLLSTFRAFL SSHLQDLSTV VRKAERYSLP IVNLKGQVLF NNWESIFSGD
GGQFNTHVPI YSFDGRDVMT DPSWPQKVVW HGSSTHGVRL VDKYCEAWRA SDMAVTGLAS
PLSSGKILDQ KAYSCANRLI VLCIENSFMT DARK
//
