ID F6PP96_MACMU Unreviewed; 1388 AA.
AC F6PP96;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 28-JAN-2026, entry version 90.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0000256|ARBA:ARBA00074723};
GN Name=COL15A1 {ECO:0000313|Ensembl:ENSMMUP00000015217.4,
GN ECO:0000313|VGNC:VGNC:103251};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000015217.4, ECO:0000313|Proteomes:UP000006718};
RN [1] {ECO:0000313|Proteomes:UP000006718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17573 {ECO:0000313|Proteomes:UP000006718};
RX PubMed=17431167; DOI=10.1126/science.1139247;
RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA Kuhn R.M., Smith K.E., Zwieg A.S.;
RT "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL Science 316:222-234(2007).
RN [2] {ECO:0000313|Ensembl:ENSMMUP00000015217.4}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000015217.4};
RA Graves T., Eichler E.E., Wilson R.K.;
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSMMUP00000015217.4}
RP IDENTIFICATION.
RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000015217.4};
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [4] {ECO:0000313|Ensembl:ENSMMUP00000015217.4}
RP IDENTIFICATION.
RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000015217.4};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_028690861.1; XM_028835028.1.
DR SMR; F6PP96; -.
DR PaxDb; 9544-ENSMMUP00000015216; -.
DR Ensembl; ENSMMUT00000016236.4; ENSMMUP00000015217.4; ENSMMUG00000011582.4.
DR GeneID; 715003; -.
DR KEGG; mcc:715003; -.
DR CTD; 1306; -.
DR VEuPathDB; HostDB:ENSMMUG00000011582; -.
DR VGNC; VGNC:103251; COL15A1.
DR eggNOG; KOG3546; Eukaryota.
DR GeneTree; ENSGT00940000164061; -.
DR HOGENOM; CLU_004003_0_0_1; -.
DR OrthoDB; 10060752at2759; -.
DR Proteomes; UP000006718; Chromosome 15.
DR Bgee; ENSMMUG00000011582; Expressed in fibroblast and 19 other cell types or tissues.
DR ExpressionAtlas; F6PP96; 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:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-ARBA.
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; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF891; COLLAGEN ALPHA-1(XVII) 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:UP000006718};
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..1388
FT /note="Collagen alpha-1(XV) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5023881690"
FT DOMAIN 40..228
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 89..227
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 223..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 989..1014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1028..1129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..420
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..540
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..570
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..609
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..630
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..731
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..780
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1045
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1107
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1117..1126
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1388 AA; 141814 MW; 9142EEE2EA213568 CRC64;
MAPRRNNGQC WCLLMLLSVS TPLPAVTQTR AATESASQGH LDLTQLIGVP LPSSVSFVTG
YGGFPAYSFG PGANVGRPAR TLIPSTFFRD FAISVMVKPS STHGGVLFAI TDAFQKVIYL
GLRLSGVEDG HQRVILYYTE PGSHVSQEAA AFSVPVMTHR WNRFAVIVQG EEVALLVDCE
EHSRIPFQRS PQALTFESSA GIFVGNAGAT GLERFTGSLQ QLTVHPDPRT PEELCDPEES
SASGETSGLQ EADGVAEILE AVTYTQAPPK EAKVEPINTP PTPSSPFEDM ELSGEPVPEG
TPETTNMSII QHSSPEQGSG EILNDTLEGI HSVDGDPITD SGSGSGAFLD IAEEKNLAAT
AVGLAEAPIS TAGEAEAGSV PTRGPTLSVS TQNPEEGVTP GPDNEETLAA TAAGEAEALA
STPWEAEASG VPPGEPDLSM SPQSLGEEAA VGPSSEGSLT TAAAATEVSL STFEDEEASG
VPTDGLAPLT ATMTPEQAVT SGPGDEEDLA AATTEEPLIT ARGEESGSPP PDGPPLPLPT
LAPERRVTPA QREHVGMKGQ AEPKGEKGDA GEEIPGPPEP SGPVGPTAGA EAEGSGLGWG
LDVGSGSGDL VGSEELLRGP PGPPGPPGLP GIPGKPGTDV FMGPPGSPGE DGRAGEPGPP
GPEGQPGVDG ATGLPGMKGE KGARGPNGSV GEKGDPGNRG LPGPPGKKGQ AGPPGAMGPP
GPPGPPGPPG PGCTMGLGFE DTEGSGSTQL LSEPKLSRPT AAIGPKGEKG DRGPKGERGT
DGASIVGPPG PRGPPGRIEV LSSSLINITH GFMNFSDIPE LVGPPGPDGL PGLPGFPGPR
GPKGDTGLPG FPGLKGEQGE KGEPGAILTG DIPLERLMGK KGEPGMHGAP GPMGPKGPPG
HKGEFGLPGR PGRPGLNGLK GAKGDPGVIM QGPPGLPGPP GPPGPPGAVI NIKGAIFPIP
IRPHCKMPVD TAHPGSPELI TFHGVKGEKG SWGLPGSKGE KGDQGAQGPP GPPLDLAYLR
HFLNNLKGEN GDKGFKGEKG EKGDINDGFL MSGPPGLPGN PGLAGQKGET VVGPQGPPGA
PGLPGPPGFG RPGDPGPPGP PGPPGPPAIL GAAVALPGPP GPPGQPGLPG SRNLVTAFSN
MDDMLQKAHL VIEGTFIYLR DSTEFFIRVR DGWKKLQLGE LIPIPADSPP PPALSSNPHQ
LLPPPNPISS TNYEKPALHL AALNMPFSGD IRADFQCFKQ ARAAGLLSTY RAFLSSHLQD
LSTIVRKAER YSLPIVNLKG QVLFNNWDSI FSGHGGQFNM HIPIYSFDGR DVMTDPSWPQ
KVIWHGSSPH GVRLVDNYCE AWRTTDTAVT GLASPLSTGK ILDQKAYSCA NRLIVLCIEN
SFMTDARK
//
