ID F1SSE8_PIG Unreviewed; 1359 AA.
AC F1SSE8;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 4.
DT 28-JAN-2026, entry version 87.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0000256|ARBA:ARBA00074723};
GN Name=COL15A1 {ECO:0000313|Ensembl:ENSSSCP00000005773.4,
GN ECO:0000313|VGNC:VGNC:86866};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000005773.4, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000005773.4}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000005773.4};
RX PubMed=32543654;
RA Warr A., Affara N., Aken B., Beiki H., Bickhart D.M., Billis K., Chow W.,
RA Eory L., Finlayson H.A., Flicek P., Giron C.G., Griffin D.K., Hall R.,
RA Hannum G., Hourlier T., Howe K., Hume D.A., Izuogu O., Kim K., Koren S.,
RA Liu H., Manchanda N., Martin F.J., Nonneman D.J., O'Connor R.E.,
RA Phillippy A.M., Rohrer G.A., Rosen B.D., Rund L.A., Sargent C.A.,
RA Schook L.B., Schroeder S.G., Schwartz A.S., Skinner B.M., Talbot R.,
RA Tseng E., Tuggle C.K., Watson M., Smith T.P.L., Archibald A.L.;
RT "An improved pig reference genome sequence to enable pig genetics and
RT genomics research.";
RL Gigascience 9:giaa051-giaa051(2020).
RN [3] {ECO:0000313|Ensembl:ENSSSCP00000005773.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [4] {ECO:0000313|Ensembl:ENSSSCP00000005773.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 SMR; F1SSE8; -.
DR FunCoup; F1SSE8; 182.
DR STRING; 9823.ENSSSCP00000005773; -.
DR GlyGen; F1SSE8; 3 sites.
DR Ensembl; ENSSSCT00000005920.5; ENSSSCP00000005773.4; ENSSSCG00000005380.5.
DR VGNC; VGNC:86866; COL15A1.
DR GeneTree; ENSGT00940000158302; -.
DR HOGENOM; CLU_1151503_0_0_1; -.
DR InParanoid; F1SSE8; -.
DR Reactome; R-SSC-1442490; Collagen degradation.
DR Reactome; R-SSC-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-SSC-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-SSC-8948216; Collagen chain trimerization.
DR Proteomes; UP000008227; Chromosome 1.
DR Bgee; ENSSSCG00000005380; Expressed in subcutaneous adipose tissue and 38 other cell types or tissues.
DR ExpressionAtlas; F1SSE8; baseline and differential.
DR GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00247; Endostatin-like; 1.
DR CDD; cd00110; LamG; 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 1: Evidence at protein level;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
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 Proteomics identification {ECO:0007829|PeptideAtlas:F1SSE8};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
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..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1359
FT /note="Collagen alpha-1(XV) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5023843593"
FT DOMAIN 39..227
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 88..226
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 222..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..990
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 524..533
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..569
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..605
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..671
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..706
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..755
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..815
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..861
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..895
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..916
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1017
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1022..1036
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1047..1079
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1098
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1359 AA; 138590 MW; B6DC47B073445D78 CRC64;
MASGRDAQCW RLLLLLSISA LLPAVTRTRS ATELASQGHL DLTELIGVPL PSSVSFVTGY
GGFPAYSFGP GANVGRPART LIPPTFFRDF AISVTVKPSS ARGGVLFAIT DAFQKVIYLG
LRLSAVEDGR QRVILYYTEP GSQVSHEAAS FPVPVMTHRW NRFAVVVQGE EASLLVECEE
QGHVSFPRSS QALAFEPSAG IFVGNAGATG LERFTGSIQQ LTVHSDPRTP EELCEAEESS
ASGEASGLQE TDGVAEMVEA VTYTQAPSEP AEVEPINMPP TPSPLSEDAE LSGEPVPEGT
QGTTNLSAFP HSSPEQGSGE ILNDTLERVH TVDGAPVTDT GSGDGAFLHV IEESLAATAA
AVESEVTIST AGEAETESVP TEGPTLSMST KDPGEEVTLG PDDEEGSAVT AAEEAEVLVS
SPGEAEAGSV PTGELTLSMS TQDPGEGGPV HEESLTTAVT AKAPLSTFEE EASRVPTDGL
APLIPTVAPE QVFTSGPGDD DLAAAATEEP LISSGAEELS GVPPEGPPLP LPTVAPERGG
APGEEGEGLP GPPPPTRPAG PTAGAEAEGS SLGWGLDIGS GSGDPVRSEE LLRGPPGPPG
PPGLPGIPGR PGTDVFVGPP GSPGEDGPAG EPGPPGPEGK PGLDGASGLP GMKGEKGARG
PDGSVGEKGD PGSRGLPGPP GKNGQVGTPG VMGPPGPPGP PGPPGPGCAM GQGFEDTEGS
GSIRLLHEPR ISGPVASVGP KGEKGDQGPK GERGMDGASI VGPPGPRGPP GRIEVLSSSL
INITHGFMNL SDIPELVGPP GPEGIPGLPG FPGPRGPKGD TGVPGFPGLK GEQGEKGEPG
AILTGDVPLE RLRGKKGEPG EHGAPGPMGP KGPPGHKGEF GLPGRPGRPG LNGLKGAKGD
RGVMMPGPPG LPGPPGPPGP PGAVINIKGA VFPIPVRPHC KTPVGTTHPG NSELITFHGV
KGEKGSWGLP GSKGEKGDQG AQGPPGPPVD PAYLRHFLNS LKGENGDRGM KGEKGDTYEG
FSVSGPPGLP GSPGLVGQKG ETVIGPQGPP GVPGLPGPPG FGRPGSPGPP GPPGPPGPPA
ILGAAVALPG PPGPPGQPGL PGSRNLVTAF SNMDDMLQKA HLVIEGTFIY LRDSTEFFIR
VRDGWKKLQL GELIPLPADS LPPPALSGNP HQPQLPLTSI SSVNYDRPAL HLVALNTPSS
GDLRADFQCF QQARAAGLLS TYRAFLSSHL QDLSTIVRKA ERYSLPIVNL KGQVLFNNWD
SIFSGHGGQF NTHVPIYSFD GRDVMTDPSW PQKVVWHGSS THGVRLVDQY CEAWRTADVA
VMLGSPLSTG KILDQKAYSC ADRLIVLCIE NSFMTDARK
//
