ID A0A2K5X6Z4_MACFA Unreviewed; 1374 AA.
AC A0A2K5X6Z4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 28-JAN-2026, entry version 42.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0000256|ARBA:ARBA00074723};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000045216.2, ECO:0000313|Proteomes:UP000233100};
RN [1] {ECO:0000313|Ensembl:ENSMFAP00000045216.2, ECO:0000313|Proteomes:UP000233100}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMFAP00000045216.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSMFAP00000045216.2}
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; ENSMFAT00000019520.2; ENSMFAP00000045216.2; ENSMFAG00000000325.2.
DR VEuPathDB; HostDB:ENSMFAG00000000325; -.
DR GeneTree; ENSGT00940000164061; -.
DR Proteomes; UP000233100; Chromosome 15.
DR Bgee; ENSMFAG00000000325; Expressed in heart and 9 other cell types or tissues.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-ARBA.
DR GO; GO:0005594; C:collagen type IX trimer; IEA:TreeGrafter.
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:SF1077; COLLAGEN ALPHA-3(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:UP000233100};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 26..214
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 75..213
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 209..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 812..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 975..1000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1014..1115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..408
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..526
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..556
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..595
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..616
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..717
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..766
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..826
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1031
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1061..1093
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1103..1112
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1374 AA; 140231 MW; B3F5CEE12051922C CRC64;
MLFSVSTPLP AVTQTRAATE SASQGHLDLT QLIGVPLPSS VSFVTGYGGF PAYSFGPGAN
VGRPARTLIP STFFRDFAIS VMVKPSSTHG GVLFAITDAF QKVIYLGLRL SGVEDGHQRV
ILYYTEPGSH VSQEAAAFSV PVMTHRWNRF AVIVQGEEVA LLLDCEEHSR IPFQRSPQAL
TFESSAGIFV GNAGATGLER FTGSLQQLTV HPDPRTPEEL CDPEESSASG DTSGLQEADG
VAEILEAVTY TQAPPKEAKV EPINTPPTPS SPFEDMELSG EPVPEGTPET TNMSIIQHSS
PEQGKGAILN DTLEGIHSVD GDPITDSGSG SGAFLDIAEE KNLAATAVGL AEAPISTAGE
AEAGSVPTRG PTLSVSTQNP EEGVTPGPDN EESLAATAAG EAEALASTPW EAEASGVPPG
EPDLSMSPQS LGEEAAVGPS SEGSLTTAAA ATEVSLSTFE DEEASGVPTD GLAPLTATMT
PEQAVTSGPG DEEDLAAATT EEPLITARGE ESGSPPPDGP PLPLPTLAPE RRVTPAQREH
VGMKGQAEPK GEKGDAGEEI PGPPEPSGPV GPTTGAEAEG SGLGWGLDVG SGSGDLVGSE
ELLRGPPGPP GPPGLPGIPG KPGTDVFMGP PGSPGEDGRA GEPGPPGPEG QPGVDGATGL
PGMKGEKGAR GPNGSVGEKG DPGNRGLPGP PGKKGQAGPP GAMGPPGPPG PPGPPGPGCT
MGLGFEDTEG SGSTQLLSEP KLSRPTAAIG PKGEKGDRGP KGERGTDGAS IVGPPGPRGP
PGRIEVLSSS LINITHGFMN FSDIPELVGP PGPDGLPGLP GFPGPRGPKG DTGLPGFPGL
KGEQGEKGEP GAILTGDIPL ERLMGKKGEP GMHGAPGPMG PKGPPGHKGE FGLPGRPGRP
GLNGLKGAKG DPGVIMQGPP GLPGPPGPPG PPGAVINIKG AIFPIPIRPH CKMPVDTAHP
GSPELITFHG VKGEKGSWGL PGSKGEKGDQ GARGPPGPPL DLAYLRHFLN NLKGENGDKG
FKGEKGEKGD INDGFLMSGP PGLPGNPGLA GQKGETVVGP QGPPGAPGLP GPPGFGRPGD
PGPPGPPGPP GPPAILGAAV ALPGPPGPPG QPGLPGSRNL VTAFSNMDDM LQKAHLVIEG
TFIYLRDSTE FFIRVRDGWK KLQLGELIPI PADSPPPPAL SSNPHQLLPP PNPISSTNYE
KPALHLAALN MPFSGDIRAD FQCFKQARAA GLLSTYRAFL SSHLQDLSTI VRKAERYSLP
IVNLKGQVLF NNWDSIFSGH GGQFNMHIPI YSFDGRDVMT DPSWPQKVIW HGSSPHGVRL
VDNYCEAWRT TDTAVTGLAS PLSTGKILDQ KAYSCANRLI VLCIENSFMT DARK
//
