ID A0A6P6CRR6_PTEVA Unreviewed; 1448 AA.
AC A0A6P6CRR6;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 28-JAN-2026, entry version 23.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0000256|ARBA:ARBA00074723};
GN Name=COL15A1 {ECO:0000313|RefSeq:XP_023390003.1};
OS Pteropus vampyrus (Large flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yinpterochiroptera; Pteropodoidea;
OC Pteropodidae; Pteropodinae; Pteropus.
OX NCBI_TaxID=132908 {ECO:0000313|Proteomes:UP000515202, ECO:0000313|RefSeq:XP_023390003.1};
RN [1] {ECO:0000313|RefSeq:XP_023390003.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_023390003.1};
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_023390003.1; XM_023534235.1.
DR GeneID; 105296289; -.
DR KEGG; pvp:105296289; -.
DR CTD; 1306; -.
DR OrthoDB; 10060752at2759; -.
DR Proteomes; UP000515202; Unplaced.
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:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
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 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 Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF912; COLLAGEN ALPHA-1(XV) CHAIN; 1.
DR Pfam; PF01391; Collagen; 2.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119,
KW ECO:0000313|RefSeq:XP_023390003.1};
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 Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000515202};
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..1448
FT /note="Collagen alpha-1(XV) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5028051019"
FT DOMAIN 1295..1448
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 223..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 904..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 963..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..248
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..386
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..442
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..545
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..565
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..666
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..715
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 986..1018
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1028..1037
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1322
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1448 AA; 151076 MW; 330F6DA924046076 CRC64;
MAPRRNVQGW RLPWLLWVSA LLAAATRSRA ATDSASQGHL DLTELVGVPL PSSVSFVTGY
GGFPAYSFGP GANVGRPART LIPPTFFRDF AISVTAKPSS TRGGVLFAIT DALQKIIYLG
LRLSGVEDGH QRVILYYTEP GSRVSHEAAA FSVPVMTHRW NRFAVTVQDE EVTLIMDCEE
HGHIPFQRSS QALAFEPSAG IFVGNAGATG LERFTGSIQQ LTIHPDPRTP EELCEAEESS
ASGETSGLQE TVGVAEILEA DTYTQAPYKE AEVNPINTPP TLSPPSEDVE LSGEPIPEGT
QETTNLSVVL HSIPEQGCGE ILNDTREGVR TVDGAPITDI GSGCGAFPQG TEEGPHTEDG
LAATAAAGEA EVTTSTTRET EVTVSTAGEA EVIVSPAEEA EASSVPTEVP ALSMTTEDPG
EKLTLGPDTE EGSGATAAGE AEMPASSDWE AEAGSVPTGG PALSMSTQES GEGVALGPVS
EGSLTTAAAA MEVSLSTFKE EEATDGLAPL MATAAPGQAV TFVGAEAEGS GLDWGSDVGS
GSGDLVRSEE LLRGPPGPPG PPGLPGIPGK PGTDVSPGPP GSPGEDGAAG EPGPPGPEGQ
PGLDGASGLP GMKGEKGARG PNGSVGEKGD PGNRGSPGPP GKNGQVGTPG IMGPPGPPGP
PGPPGPGCTM GLGFEDTEGS GSIRLLHEPR ISGPMASNGP KGEKGDPGPK GDRGMDGASI
VGPPGPRGPP GHLKVLSNWG WRDRVKTTGL GEPLDKMVRR MLDFTERFSE LQGEKGEPGA
ILTGDIPLER LRGEKGEPGV HGTPGPMGPK GPPGHKGEFG LPGRPGRPGL NGLKGTKGDR
GIMMPGPPGL PGPPGPPGPP GAVVNIKGAV FPIPARPHCK TPVGTTHPGN SELITFHGVK
GEKGSWGLPG SKGEKGDQGA QGPPGPPVDP AYLRHFLNSL KGENGDRGFK GEKGDSIVDF
SMSGPPGLPG SPGLVGQKGE TIVGPQGPPG VPGMPGPPGF GRPGPPGPPG PPGPPGPPAI
LGAAVALPGP PGPPGQPGIP GSRNLVTAFS NMDDMLQKAH LVIEGTFIYL RDSTEFFIRV
RDGWKKLQLG ELIPIPADSP PPPALSSNPH SLQSQLTSIS SVNYERPALH LIALNMPFSG
DVRADYQCFQ QARAAGLLST YRAFLSSHLQ DLSTVVRKAE RYSLPIVNLK GQILFNNWDS
IFSGHGGQFS TRVPIYSFDG RDVMTDPSWP QKVIWHGSST HGVRLVDKYC EAWRTADMAV
TGLASPLSTG KILDQKAYSC ASLPLLVQRT IARTIVLQES IGKGRFGEVW RGKWRGEEVA
VKIFSSREER SWFREAEIYQ TVMLRHENIL GFIAADNKAV NIISANSMKL KKLENGDIVE
KQVNENLEMP PFSKDGGKVK IRVITSKVRV VKRLEFHLCY NYFETFAHTV CYEDIWPEGI
LTLLKQQQ
//
