ID A0A2K6P950_RHIRO Unreviewed; 488 AA.
AC A0A2K6P950;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Fibulin-5 {ECO:0000256|ARBA:ARBA00021559};
GN Name=FBLN5 {ECO:0000313|Ensembl:ENSRROP00000013082.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000013082.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000013082.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR AlphaFoldDB; A0A2K6P950; -.
DR STRING; 61622.ENSRROP00000013082; -.
DR Ensembl; ENSRROT00000037205.1; ENSRROP00000013082.1; ENSRROG00000030805.1.
DR GeneTree; ENSGT00940000158774; -.
DR Proteomes; UP000233200; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0048251; P:elastic fiber assembly; IEA:Ensembl.
DR GO; GO:0046903; P:secretion; IEA:Ensembl.
DR CDD; cd00054; EGF_CA; 1.
DR Gene3D; 2.10.25.10; Laminin; 6.
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; IPR009030; Growth_fac_rcpt_cys_sf.
DR PANTHER; PTHR24034; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24034:SF107; FIBULIN-5; 1.
DR Pfam; PF12662; cEGF; 3.
DR Pfam; PF07645; EGF_CA; 2.
DR PRINTS; PR00907; THRMBOMODULN.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00179; EGF_CA; 6.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 4.
DR PROSITE; PS01186; EGF_2; 4.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS01187; EGF_CA; 2.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Reference proteome {ECO:0000313|Proteomes:UP000233200};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..488
FT /note="Fibulin-5"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014424630"
FT DOMAIN 167..207
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 208..246
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 247..286
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 287..327
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 251..261
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 488 AA; 54233 MW; F9EBD94D132A42FF CRC64;
MPGKFLILTV TILALCLPSP GNAQAQCTNG FDLDRQSGQC LAFSLLLLKL ECSGTILARC
NLRLLVSSDS SASASQVAGI TDIDECRTIP EACRGDMMCV NQNGGYLCIP RTNPVYRGPY
SNPYSTPYSG PYPAAAPPLS APNYPTISRP LICRFGYQMD EGNQCVDVDE CATDSHQCNP
TQICINTEGG YTCSCTDGYW LLEGQCLDID ECRYGYCQQL CANVPGSYSC TCNPGFTLNE
DGRSCQDVNE CATENPCVQT CVNTYGSFIC RCDPGYELEE DGVHCSDMDE CSFSEFLCQH
ECVNQPGTYF CSCPPGYILL DDNRSCQDIN ECEHRNHTCN LQQTCYNLQG GFKCIDPIRC
EEPYLRISDN RCMCPAENPG CRDQPFTILY RDMDVVSGRS VPADIFQMQA TTRYPGAYYI
FQIKSGNEGR EFYMRQTGPI SATLVMTRPI KGPREIQLDL EMITVNTVIN FRGSSVIRLR
IYVSQYPF
//
