FBP1_STRPU
ID FBP1_STRPU Reviewed; 1064 AA.
AC P10079;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 25-MAY-2022, entry version 149.
DE RecName: Full=Fibropellin-1;
DE AltName: Full=Epidermal growth factor-related protein 1;
DE AltName: Full=Fibropellin-I;
DE AltName: Full=SpEGF I;
DE AltName: Full=UEGF-1;
DE Flags: Precursor;
GN Name=EGF1;
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 [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX PubMed=2514273; DOI=10.1007/bf02103619;
RA Delgadillo-Reynoso M.G., Rollo D.R., Hursh D.A., Raff R.A.;
RT "Structural analysis of the uEGF gene in the sea urchin strongylocentrotus
RT purpuratus reveals more similarity to vertebrate than to invertebrate genes
RT with EGF-like repeats.";
RL J. Mol. Evol. 29:314-327(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 279-476 AND 781-1064.
RX PubMed=3498216; DOI=10.1126/science.3498216;
RA Hursh D.A., Andrews M.E., Raff R.A.;
RT "A sea urchin gene encodes a polypeptide homologous to epidermal growth
RT factor.";
RL Science 237:1487-1490(1987).
RN [3]
RP DOMAIN AVIDIN-LIKE.
RX PubMed=2784773; DOI=10.1096/fasebj.3.6.2784773;
RA Hunt L.T., Barker W.C.;
RT "Avidin-like domain in an epidermal growth factor homolog from a sea
RT urchin.";
RL FASEB J. 3:1760-1764(1989).
RN [4]
RP CHARACTERIZATION.
RX PubMed=2060714; DOI=10.1016/0012-1606(91)90449-d;
RA Bisgrove B.W., Andrews M.E., Raff R.A.;
RT "Fibropellins, products of an EGF repeat-containing gene, form a unique
RT extracellular matrix structure that surrounds the sea urchin embryo.";
RL Dev. Biol. 146:89-99(1991).
RN [5]
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. Cytoplasmic
CC vesicle. Secreted, extracellular space, extracellular matrix, hyaline
CC layer. Secreted, extracellular space, extracellular matrix, apical
CC lamina. Note=In vesicles in the cytoplasm of unfertilized eggs, then to
CC the base of the hyaline layer throughout development and finally in the
CC apical lamina in late embryos and early larvae.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Ia;
CC IsoId=P10079-1; Sequence=Displayed;
CC Name=Ib;
CC IsoId=P10079-2; Sequence=VSP_000451;
CC -!- DEVELOPMENTAL STAGE: Moderate levels in unfertilized eggs and during
CC early cleavage, then rapidly increases in abundance between late morula
CC and mesenchyme blastula stages to maximal levels maintained through
CC subsequent stages. Expressed both maternally and zygotically.
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DR EMBL; L08692; AAA62164.1; -; Genomic_DNA.
DR EMBL; L08692; AAA62163.1; -; Genomic_DNA.
DR EMBL; X17530; CAA35571.1; -; mRNA.
DR EMBL; M17421; AAA30050.1; -; mRNA.
DR EMBL; X17533; CAA35573.1; -; mRNA.
DR PIR; A40136; A40136.
DR RefSeq; NP_001229629.1; NM_001242700.1. [P10079-1]
DR AlphaFoldDB; P10079; -.
DR SMR; P10079; -.
DR TCDB; 9.B.87.1.28; the selenoprotein p receptor (selp-receptor) family.
DR EnsemblMetazoa; NM_001242700; NP_001229629; GeneID_373313. [P10079-1]
DR GeneID; 373313; -.
DR KEGG; spu:373313; -.
DR CTD; 373313; -.
DR eggNOG; KOG1217; Eukaryota.
DR InParanoid; P10079; -.
DR OrthoDB; 561378at2759; -.
DR Proteomes; UP000007110; Unassembled WGS sequence.
DR GO; GO:0032579; C:apical lamina of hyaline layer; IEA:UniProtKB-SubCell.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
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; IPR013032; EGF-like_CS.
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; 18.
DR Pfam; PF12661; hEGF; 3.
DR PRINTS; PR00709; AVIDIN.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00181; EGF; 21.
DR SMART; SM00179; EGF_CA; 21.
DR SUPFAM; SSF49854; SSF49854; 1.
DR SUPFAM; SSF50876; SSF50876; 1.
DR SUPFAM; SSF57184; SSF57184; 5.
DR PROSITE; PS00010; ASX_HYDROXYL; 19.
DR PROSITE; PS00577; AVIDIN_1; 1.
DR PROSITE; PS51326; AVIDIN_2; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS00022; EGF_1; 19.
DR PROSITE; PS01186; EGF_2; 19.
DR PROSITE; PS50026; EGF_3; 21.
DR PROSITE; PS01187; EGF_CA; 18.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cytoplasmic vesicle; Disulfide bond;
KW EGF-like domain; Extracellular matrix; Glycoprotein; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1064
FT /note="Fibropellin-1"
FT /id="PRO_0000002732"
FT DOMAIN 20..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; calcium-binding"
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 442..478
FT /note="EGF-like 9; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 480..516
FT /note="EGF-like 10; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 518..554
FT /note="EGF-like 11; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 556..592
FT /note="EGF-like 12; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 594..630
FT /note="EGF-like 13; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 632..668
FT /note="EGF-like 14; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 670..706
FT /note="EGF-like 15; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 708..744
FT /note="EGF-like 16; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 746..782
FT /note="EGF-like 17; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 784..820
FT /note="EGF-like 18; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 822..858
FT /note="EGF-like 19; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 860..896
FT /note="EGF-like 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 898..934
FT /note="EGF-like 21; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 937..1056
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 851
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"
FT DISULFID 446..457
FT /evidence="ECO:0000250"
FT DISULFID 451..466
FT /evidence="ECO:0000250"
FT DISULFID 468..477
FT /evidence="ECO:0000250"
FT DISULFID 484..495
FT /evidence="ECO:0000250"
FT DISULFID 489..504
FT /evidence="ECO:0000250"
FT DISULFID 506..515
FT /evidence="ECO:0000250"
FT DISULFID 522..533
FT /evidence="ECO:0000250"
FT DISULFID 527..542
FT /evidence="ECO:0000250"
FT DISULFID 544..553
FT /evidence="ECO:0000250"
FT DISULFID 560..571
FT /evidence="ECO:0000250"
FT DISULFID 565..580
FT /evidence="ECO:0000250"
FT DISULFID 582..591
FT /evidence="ECO:0000250"
FT DISULFID 598..609
FT /evidence="ECO:0000250"
FT DISULFID 603..618
FT /evidence="ECO:0000250"
FT DISULFID 620..629
FT /evidence="ECO:0000250"
FT DISULFID 636..647
FT /evidence="ECO:0000250"
FT DISULFID 641..656
FT /evidence="ECO:0000250"
FT DISULFID 658..667
FT /evidence="ECO:0000250"
FT DISULFID 674..685
FT /evidence="ECO:0000250"
FT DISULFID 679..694
FT /evidence="ECO:0000250"
FT DISULFID 696..705
FT /evidence="ECO:0000250"
FT DISULFID 712..723
FT /evidence="ECO:0000250"
FT DISULFID 717..732
FT /evidence="ECO:0000250"
FT DISULFID 734..743
FT /evidence="ECO:0000250"
FT DISULFID 750..761
FT /evidence="ECO:0000250"
FT DISULFID 755..770
FT /evidence="ECO:0000250"
FT DISULFID 772..781
FT /evidence="ECO:0000250"
FT DISULFID 788..799
FT /evidence="ECO:0000250"
FT DISULFID 793..808
FT /evidence="ECO:0000250"
FT DISULFID 810..819
FT /evidence="ECO:0000250"
FT DISULFID 826..837
FT /evidence="ECO:0000250"
FT DISULFID 831..846
FT /evidence="ECO:0000250"
FT DISULFID 848..857
FT /evidence="ECO:0000250"
FT DISULFID 864..875
FT /evidence="ECO:0000250"
FT DISULFID 869..884
FT /evidence="ECO:0000250"
FT DISULFID 886..895
FT /evidence="ECO:0000250"
FT DISULFID 902..913
FT /evidence="ECO:0000250"
FT DISULFID 907..922
FT /evidence="ECO:0000250"
FT DISULFID 924..933
FT /evidence="ECO:0000250"
FT VAR_SEQ 477..780
FT /note="Missing (in isoform Ib)"
FT /evidence="ECO:0000305"
FT /id="VSP_000451"
FT CONFLICT 279
FT /note="L -> S (in Ref. 2; AAA30050)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1064 AA; 112073 MW; 2E569CA012ED6D09 CRC64;
MRTWLLAVLL LSVIAVTYGQ GECDSDPCEN GSTCQEGEGS YICQCPMGYD GQNCDRFTGS
NCGYNVFDAN GMIDSPNYPA MYNNRADCLY LVRITKARSI TFTIEDFMTE VFKDVVEYGI
GPEADFNQAL GSFEGNLTQD DVIPAPFTVQ GDQAWFIFST DRNIVNRGFR ITFSSDGDDC
DPNLCQNGAA CTDLVNDYAC TCPPGFTGRN CEIDIDECAS DPCQNGGACV DGVNGYVCNC
VPGFDGDECE NNINECASSP CLNGGICVDG VNMFECTCLA GFTGVRCEVN IDECASAPCQ
NGGICIDGIN GYTCSCPLGF SGDNCENNDD ECSSIPCLNG GTCVDLVNAY MCVCAPGWTG
PTCADNIDEC ASAPCQNGGV CIDGVNGYMC DCQPGYTGTH CETDIDECAR PPCQNGGDCV
DGVNGYVCIC APGFDGLNCE NNIDECASRP CQNGAVCVDG VNGFVCTCSA GYTGVLCETD
INECASMPCL NGGVCTDLVN GYICTCAAGF EGTNCETDTD ECASFPCQNG ATCTDQVNGY
VCTCVPGYTG VLCETDINEC ASFPCLNGGT CNDQVNGYVC VCAQDTSVST CETDRDECAS
APCLNGGACM DVVNGFVCTC LPGWEGTNCE INTDECASSP CMNGGLCVDQ VNSYVCFCLP
GFTGIHCGTE IDECASSPCL NGGQCIDRVD SYECVCAAGY TAVRCQINID ECASAPCQNG
GVCVDGVNGY VCNCAPGYTG DNCETEIDEC ASMPCLNGGA CIEMVNGYTC QCVAGYTGVI
CETDIDECAS APCQNGGVCT DTINGYICAC VPGFTGSNCE TNIDECASDP CLNGGICVDG
VNGFVCQCPP NYSGTYCEIS LDACRSMPCQ NGATCVNVGA DYVCECVPGY AGQNCEIDIN
ECASLPCQNG GLCIDGIAGY TCQCRLGYIG VNCEEVGFCD LEGMWYNECN DQVTITKTST
GMMLGDYMTY NERALGYAAP TVVVGYASNN YDFPSFGFTV VRDNGQSTTS WTGQCHLCDG
EEVLYTTWIN TNMVSTCQDI KKSNMVGQDK WTRYEQSIAP QPDA
