ID A0A3Q7UZZ7_VULVU Unreviewed; 678 AA.
AC A0A3Q7UZZ7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Fibulin-1 {ECO:0000256|ARBA:ARBA00021554, ECO:0000256|PIRNR:PIRNR036313};
GN Name=FBLN1 {ECO:0000313|RefSeq:XP_025873115.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025873115.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025873115.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025873115.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025873115.1};
RG RefSeq;
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}.
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DR RefSeq; XP_025873115.1; XM_026017330.1.
DR AlphaFoldDB; A0A3Q7UZZ7; -.
DR Proteomes; UP000286640; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016504; F:peptidase activator activity; IEA:InterPro.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:InterPro.
DR CDD; cd00017; ANATO; 2.
DR CDD; cd00054; EGF_CA; 5.
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:SF97; FIBULIN-1; 1.
DR Pfam; PF01821; ANATO; 2.
DR Pfam; PF12662; cEGF; 3.
DR Pfam; PF07645; EGF_CA; 4.
DR PIRSF; PIRSF036313; Fibulin-1; 1.
DR SMART; SM00104; ANATO; 3.
DR SMART; SM00181; EGF; 9.
DR SMART; SM00179; EGF_CA; 8.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF57184; Growth factor receptor domain; 3.
DR PROSITE; PS01177; ANAPHYLATOXIN_1; 1.
DR PROSITE; PS01178; ANAPHYLATOXIN_2; 3.
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:UP000286640};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|PIRNR:PIRNR036313}.
FT DOMAIN 28..61
FT /note="Anaphylatoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS01178"
FT DOMAIN 69..102
FT /note="Anaphylatoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS01178"
FT DOMAIN 104..136
FT /note="Anaphylatoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS01178"
FT DOMAIN 351..393
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 394..435
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 436..475
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 476..519
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
SQ SEQUENCE 678 AA; 74223 MW; 74B69E7A995EEFF6 CRC64;
MGPWRVTPRP GTLLSPHTVA ADTVMEACCA DGHQMATQHR DCSLPYTSES KECRMVQEQC
CHSQLEELHC ATGINLANEQ DSCATSHGDN TSLEATFVKR CCHCCLLGRA AQAQGQSCEY
TLMVGYQCGL VFRACCVKGQ ETADFAPGDI GDLQEAAKIS EIEEEQEDPY LNDRCRGGGP
CKQQCRDTGE EVVCSCFVGY QLLPDSVSCE DINECITGNH NCRLGESCVN TVGSFRCQRD
SSCGTGYELT EDNDCKDIDE CESGIHNCLP DFICQNTLGS FRCRPKLQCK SGFIQDALGN
CIDINECLSI SAPCPVGQTC INTEGSYTCQ KNVPNCGRGY HLNEEGTRCV DVDECAAPSE
PCGPGHLCVN SPGSFRCECK AGYYFDGISR TCVDINECRR YPGRLCGHKC ENTPGSYFCS
CTMGFRLSAD GRSCEDVNEC SSSPCSQECA NVYGSYQCYC RRGYQLSDVD GVTCEDIDEC
ALPTGGHICS YRCINIPGSF QCSCPSSGYR LAPNGRNCQD IDECVTGIHN CSINETCFNI
QGGFRCLAFE CPKNYRRSAD TRCERLPCHE TQECPKLPLR ITYYHLSFPT NIQVPAVVFR
MGPSNAVPGD SMQLAIVGGN EEGFFTTRKV SHHSGVVALT KPVPEPRDLL LTVKMDLYRH
GTVSSFVAKL YIFVSAEL
//
