FBP3_STRPU
ID FBP3_STRPU Reviewed; 570 AA.
AC P49013;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Fibropellin-3;
DE AltName: Full=Epidermal growth factor-related protein 3;
DE AltName: Full=Fibropellin III;
DE AltName: Full=Fibropellin-c;
DE AltName: Full=SpEGF III;
DE Flags: Precursor;
GN Name=EGF3;
OS Strongylocentrotus purpuratus (Purple sea urchin).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC Euechinoidea; Echinacea; Camarodonta; Echinidea; Strongylocentrotidae;
OC Strongylocentrotus.
OX NCBI_TaxID=7668;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=8500658; DOI=10.1006/dbio.1993.1155;
RA Bisgrove B.W., Raff R.A.;
RT "The SpEGF III gene encodes a member of the fibropellins: EGF repeat-
RT containing proteins that form the apical lamina of the sea urchin embryo.";
RL Dev. Biol. 157:526-538(1993).
RN [2]
RP SUBUNIT, AND ABSENCE OF BINDING TO AVIDIN.
RX PubMed=15659374; DOI=10.1110/ps.04898705;
RA Yanai I., Yu Y., Zhu X., Cantor C.R., Weng Z.;
RT "An avidin-like domain that does not bind biotin is adopted for
RT oligomerization by the extracellular mosaic protein fibropellin.";
RL Protein Sci. 14:417-423(2005).
CC -!- FUNCTION: Forms the apical lamina, a component of the extracellular
CC matrix.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|PROSITE-ProRule:PRU00656,
CC ECO:0000269|PubMed:15659374}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- DEVELOPMENTAL STAGE: Low levels in unfertilized eggs and during early
CC cleavage, then rapidly increases in abundance between late morula and
CC mesenchyme blastula stages to maximal levels maintained through
CC subsequent stages.
CC -!- MISCELLANEOUS: Expressed both maternally and zygotically.
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DR EMBL; L07045; AAA30045.1; -; mRNA.
DR PIR; A48836; A48836.
DR RefSeq; NP_999703.1; NM_214538.1.
DR AlphaFoldDB; P49013; -.
DR SMR; P49013; -.
DR EnsemblMetazoa; NM_214538; NP_999703; GeneID_373315.
DR GeneID; 373315; -.
DR KEGG; spu:373315; -.
DR CTD; 373315; -.
DR eggNOG; KOG1217; Eukaryota.
DR InParanoid; P49013; -.
DR OrthoDB; 606546at33208; -.
DR PhylomeDB; P49013; -.
DR Proteomes; UP000007110; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0009374; F:biotin binding; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00041; CUB; 1.
DR Gene3D; 2.40.128.30; -; 1.
DR Gene3D; 2.60.120.290; -; 1.
DR InterPro; IPR005469; Avidin.
DR InterPro; IPR017889; Avidin-like_CS.
DR InterPro; IPR036896; Avidin-like_sf.
DR InterPro; IPR005468; Avidin/str.
DR InterPro; IPR000859; CUB_dom.
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 InterPro; IPR035914; Sperma_CUB_dom_sf.
DR Pfam; PF01382; Avidin; 1.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF00008; EGF; 8.
DR PRINTS; PR00709; AVIDIN.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00181; EGF; 8.
DR SMART; SM00179; EGF_CA; 8.
DR SUPFAM; SSF49854; SSF49854; 1.
DR SUPFAM; SSF50876; SSF50876; 1.
DR SUPFAM; SSF57184; SSF57184; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 8.
DR PROSITE; PS00577; AVIDIN_1; 1.
DR PROSITE; PS51326; AVIDIN_2; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS00022; EGF_1; 8.
DR PROSITE; PS01186; EGF_2; 7.
DR PROSITE; PS50026; EGF_3; 8.
DR PROSITE; PS01187; EGF_CA; 6.
PE 1: Evidence at protein level;
KW Calcium; Disulfide bond; EGF-like domain; Glycoprotein; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..570
FT /note="Fibropellin-3"
FT /id="PRO_0000002733"
FT DOMAIN 18..55
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 62..175
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 176..212
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 214..250
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 252..288
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 290..326
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 328..364
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 366..402
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 404..440
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 443..562
FT /note="Avidin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00656"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 23..34
FT /evidence="ECO:0000250"
FT DISULFID 28..43
FT /evidence="ECO:0000250"
FT DISULFID 45..54
FT /evidence="ECO:0000250"
FT DISULFID 62..88
FT /evidence="ECO:0000250"
FT DISULFID 180..191
FT /evidence="ECO:0000250"
FT DISULFID 185..200
FT /evidence="ECO:0000250"
FT DISULFID 202..211
FT /evidence="ECO:0000250"
FT DISULFID 218..229
FT /evidence="ECO:0000250"
FT DISULFID 223..238
FT /evidence="ECO:0000250"
FT DISULFID 240..249
FT /evidence="ECO:0000250"
FT DISULFID 256..267
FT /evidence="ECO:0000250"
FT DISULFID 261..276
FT /evidence="ECO:0000250"
FT DISULFID 278..287
FT /evidence="ECO:0000250"
FT DISULFID 294..305
FT /evidence="ECO:0000250"
FT DISULFID 299..314
FT /evidence="ECO:0000250"
FT DISULFID 316..325
FT /evidence="ECO:0000250"
FT DISULFID 332..343
FT /evidence="ECO:0000250"
FT DISULFID 337..352
FT /evidence="ECO:0000250"
FT DISULFID 354..363
FT /evidence="ECO:0000250"
FT DISULFID 370..381
FT /evidence="ECO:0000250"
FT DISULFID 375..390
FT /evidence="ECO:0000250"
FT DISULFID 392..401
FT /evidence="ECO:0000250"
FT DISULFID 408..419
FT /evidence="ECO:0000250"
FT DISULFID 413..428
FT /evidence="ECO:0000250"
FT DISULFID 430..439
FT /evidence="ECO:0000250"
SQ SEQUENCE 570 AA; 61116 MW; BE665E3E1C05E6EE CRC64;
MKVSLLAVLL LSIVAATYGQ GECGSNPCEN GSVCRDGEGT YICECQMGYD GQNCDRFTGA
NCGYNIFEST GVIESPNYPA NYNNRADCLY LVRIKGARVI TFTIEDFATE IFKDAVEYGV
GPVADFNQAL ATFEGNLTAN NQVPPPFSVQ GEQAWFIFST DRNIPRKGFR ITFSSDGDDC
TPNPCLNGAT CVDQVNDYQC ICAPGFTGDN CETDIDECAS APCRNGGACV DQVNGYTCNC
IPGFNGVNCE NNINECASIP CLNGGICVDG INQFACTCLP GYTGILCETD INECASSPCQ
NGGSCTDAVN RYTCDCRAGF TGSNCETNIN ECASSPCLNG GSCLDGVDGY VCQCLPNYTG
THCEISLDAC ASLPCQNGGV CTNVGGDYVC ECLPGYTGIN CEIDINECAS LPCQNGGECI
NGIAMYICQC RQGYAGVNCE EVGFCDLEGV WFNECNDQIT IIKTSTGMML GDHMTFTERE
LGVAAPTVMV GYPSNNYDFP SFGITVVRDN GRTTTSWTGQ CHLCDGQEVL YTTWIESSMV
STCEEIKRAN KVGQDKWTRY EQSFAPQPDA
