ID G1PPV2_MYOLU Unreviewed; 678 AA.
AC G1PPV2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Fibulin-1 {ECO:0000256|ARBA:ARBA00021554, ECO:0000256|PIRNR:PIRNR036313};
GN Name=FBLN1 {ECO:0000313|Ensembl:ENSMLUP00000013061.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000013061.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000013061.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000013061.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Incorporated into fibronectin-containing matrix fibers. May
CC play a role in cell adhesion and migration along protein fibers within
CC the extracellular matrix (ECM). Could be important for certain
CC developmental processes and contribute to the supramolecular
CC organization of ECM architecture, in particular to those of basement
CC membranes. {ECO:0000256|PIRNR:PIRNR036313}.
CC -!- SUBUNIT: Homomultimerizes and interacts with various extracellular
CC matrix components. {ECO:0000256|PIRNR:PIRNR036313}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498, ECO:0000256|PIRNR:PIRNR036313}.
CC -!- SIMILARITY: Belongs to the fibulin family.
CC {ECO:0000256|ARBA:ARBA00006127, ECO:0000256|PIRNR:PIRNR036313}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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 EMBL; AAPE02050012; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02050013; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02050014; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02050015; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02050016; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02050017; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1PPV2; -.
DR STRING; 59463.ENSMLUP00000013061; -.
DR Ensembl; ENSMLUT00000014356.2; ENSMLUP00000013061.2; ENSMLUG00000014350.2.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000156642; -.
DR HOGENOM; CLU_004826_1_1_1; -.
DR InParanoid; G1PPV2; -.
DR OMA; DNDCKDV; -.
DR TreeFam; TF317514; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0005604; C:basement membrane; IEA:Ensembl.
DR GO; GO:0071953; C:elastic fiber; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IEA:Ensembl.
DR GO; GO:0070051; F:fibrinogen binding; IEA:Ensembl.
DR GO; GO:0001968; F:fibronectin binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0005178; F:integrin binding; IEA:Ensembl.
DR GO; GO:0016504; F:peptidase activator activity; IEA:Ensembl.
DR GO; GO:0072378; P:blood coagulation, fibrin clot formation; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
DR GO; GO:2000146; P:negative regulation of cell motility; IEA:Ensembl.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:2000647; P:negative regulation of stem cell proliferation; IEA:Ensembl.
DR GO; GO:1900025; P:negative regulation of substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR CDD; cd00017; ANATO; 1.
DR CDD; cd00054; EGF_CA; 7.
DR Gene3D; 2.10.25.10; Laminin; 9.
DR InterPro; IPR000020; Anaphylatoxin/fibulin.
DR InterPro; IPR026823; cEGF.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR017048; Fibulin-1.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR PANTHER; PTHR24034; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24034:SF166; VACUOLAR-SORTING RECEPTOR 1; 1.
DR Pfam; PF12662; cEGF; 3.
DR Pfam; PF07645; EGF_CA; 4.
DR PIRSF; PIRSF036313; Fibulin-1; 1.
DR SMART; SM00104; ANATO; 2.
DR SMART; SM00181; EGF; 9.
DR SMART; SM00179; EGF_CA; 8.
DR SUPFAM; SSF57196; EGF/Laminin; 3.
DR SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR PROSITE; PS01177; ANAPHYLATOXIN_1; 1.
DR PROSITE; PS01178; ANAPHYLATOXIN_2; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 4.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS01187; EGF_CA; 3.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530,
KW ECO:0000256|PIRNR:PIRNR036313};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000001074};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|PIRNR:PIRNR036313}.
FT DOMAIN 10..42
FT /note="Anaphylatoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS01178"
FT DOMAIN 331..373
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 374..415
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 416..455
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 456..499
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
SQ SEQUENCE 678 AA; 74360 MW; 5719DB63D81AFA3E CRC64;
ARADLSMEAC CADGHRVATQ HRDCSLPYAS SMECRMVQEQ CCHSQLEELH CATGINLANE
QDSCAVSAAN ASLEAVFVKG LTVCCLEATL RATDPCSDKG FLTSPPGLVK RARWRAGSGH
PGLCLAHGGD LVFASLKAPT EEEQEDPYND RCRGGGPCKQ QCRDTGEEVV CSCFVGYQLL
ADGVSCEDVN ECITRTHSCR LGESCINTVG SFRCQRDSSC GTGYELTEDN DCKDVPDIDE
CESGIHNCLP DFICQNTLGS FRCRPKLQCK SGFIQDALGS CIDINECLSI SPTCPVGHTC
INTEGSYTCQ KNVPNCGRGY HLNEEGTRCQ DVDECAPPSE PCGPGHLCVN SPGSFRCECK
AGFYFDGISR TCVDINECRR YSGRLCSHKC ENTLGSFHCS CSAGFRLAPD GRSCEDVNEC
TSSPCSQECA NVYGSFQCYC RRGFQLSDVD GVTCEDIDEC ALPTGGHICS YRCINFPGSF
QCSCPPTGYR LAPNGRNCQD IDECVTGIHN CSINETCFNI QGSFRCLAFE CPENYRRSAD
TLHQEKTDTV RCIKSCRPSD ISCMRDLVHT VSHTVVSLPT FREFAHPEEI IFLRAVMPAH
PANHADIIFD ITEGNLRDSF DIVKRYVDGM TVGVVRQVRP IVGPFHAVLK LEMNYVVGGV
VNHRNIVNVH IFVSEYWF
//
