ID A0A8C9AL00_PROSS Unreviewed; 1386 AA.
AC A0A8C9AL00;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0000256|ARBA:ARBA00074723};
GN Name=COL15A1 {ECO:0000313|Ensembl:ENSPSMP00000034151.1};
OS Prolemur simus (Greater bamboo lemur) (Hapalemur simus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Lemuridae; Prolemur.
OX NCBI_TaxID=1328070 {ECO:0000313|Ensembl:ENSPSMP00000034151.1, ECO:0000313|Proteomes:UP000694414};
RN [1] {ECO:0000313|Ensembl:ENSPSMP00000034151.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSPSMP00000034151.1}
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 Ensembl; ENSPSMT00000039372.1; ENSPSMP00000034151.1; ENSPSMG00000023541.1.
DR GeneTree; ENSGT00940000158302; -.
DR Proteomes; UP000694414; Unplaced.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-ARBA.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-ARBA.
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; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF714; COLLAGEN ALPHA-4(IV) CHAIN; 1.
DR Pfam; PF01391; Collagen; 3.
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};
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:UP000694414};
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..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..1386
FT /note="Collagen alpha-1(XV) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034480680"
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 265..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 882..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 994..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1051..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1185..1207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..349
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..531
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..541
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..631
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..732
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..781
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..921
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..947
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1105
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1115..1124
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1386 AA; 140929 MW; 5C747A909E75B70E CRC64;
MAPRRNGQHW CLMWLLSVSA ILSAVTQIRA ATEPASQGPL DLTALIGVPL PSSVSFVTGY
RGSPAYSFGP GANVGRPVRT LIPSTFFRDF AVSVTVKPSG AHGGVLFAIT DAFQKVIYLG
LRLSGVEDGH QRVILYYTEP GSHVSHEAAA FSVPVMTNRW NRFAVIVQDE EVTLLVDCEE
HSHIAFQRSP RPLAFEPSAG IFVGNAGATG LERFTGSIQQ LTVHPDPRKP EELCEAEEFS
ASGETSGLQE TAGVAETVEA VTYTQAPPQE AKVEPINRPP TLPSPSEDTE LSGEPVPEGT
PEATNMSVVQ HGSPEQGSGQ MLNDTLEGVH AVDGDPITDT GSGSGDGASL DVIEEKGLAT
TAAGPAEVPV STAGEAEADS VPTGGSPVSM ATQHPGEEVT PGPDDEEGSA ATAAEEAEVP
TSTAGEAEAG GVPTGGLALS TATQPPREEV TPGPNGEESL TIVAAVTEVL LSPSEDEEAS
GVPTGGLGPL TPTAAPGQAV TSVPGDEEGS AAATTEEPLT TAGAEESGSV PPDGPPLPVP
TAAPERVVTL AQTLHVGMTE QAVPKGEKGD AGEELPGSPE PFGPARPTVG EEPEGSGPVW
GLDVGSGSGD QPGSEELLRG PPGPPGPPGS PGIPGKPGTD VSTGPPGSPG EDGVAGEPGP
PGPKGQPGVD GVTGLPGMKG EKGARGPNGS VGEKGDPGNR GLPGPPGKNG QVGTPGVMGP
PGPPGPPGPP GPGCAVGLGF EDTEGSGSIS LLHEPRVSGP MAPRGPKGEK GERGPKGDRG
MDGASIVGPP GPRGPPGRVE FLSSSFINIT HGSMNFSGIP ELVGPPGPDG MPGLPGFPGP
RGPKGDTGVP GFPGLKGEQG EKGEPGAILT GDVPLERLMG KKGEPGVHGA PGPMGPKGPP
GHKGELGLPG RPGRPGLNGP KGAKGDRGVM MPGPPGLPGP PGPPGPPGAV INIKGAVFPI
PVRPHCKTPV GTTHPGNPEL ITFHGVKGEK GSWGLPGTKG EKGDQGAQGP PGPPIDPAYL
RHFLNSLKGE NGDRGFKGEK GDSNDNFFVS GPPGLPGNPG LAGQKGETVI GPQGPPGAPG
LPGPPGFGRP GVPGPPGPPG PPGPPAILGA AVALPGPPGP PGQPGLPGSR NLVTTFSNMD
DMLQKAHLVI EGTFIYLRDS TEFFIRVRDG WKKLQLGELI PIPADSPPPP ALSSNPHHPQ
PPLNPISSAN YEKPALHLVA LNMPFSGDIR ADFQCFQQAR AAGLLSTYRA FLSSHLQDLS
TVVRKAERHS LPIVNLKGQV LFNNWDSIFA GHGGQFNTHI PIYSFDGRDV MTDPSWPQKV
IWHGSSPHGV RLVDKYCEAW RTADMAVTGL ASPLSSGKIL DQKTYSCANR LIVLCIENSF
MTDARK
//
