GenomeNet

Database: UniProt
Entry: P10079
LinkDB: P10079
Original site: P10079 
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   16-JAN-2019, entry version 136.
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;
OC   Echinoidea; Euechinoidea; Echinacea; Echinoida; 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
RT   strongylocentrotus purpuratus reveals more similarity to vertebrate
RT   than to invertebrate genes 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
RT   growth factor.";
RL   Science 237:1487-1490(1987).
RN   [3]
RP   DOMAIN AVIDIN-LIKE.
RX   PubMed=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
RT   unique extracellular matrix structure that surrounds the sea urchin
RT   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
CC       extracellular 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,
CC       hyaline layer. Secreted, extracellular space, extracellular
CC       matrix, apical lamina. Note=In vesicles in the cytoplasm of
CC       unfertilized eggs, then to the base of the hyaline layer
CC       throughout development and finally in the apical lamina in late
CC       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
CC       during early cleavage, then rapidly increases in abundance between
CC       late morula and mesenchyme blastula stages to maximal levels
CC       maintained through subsequent stages. Expressed both maternally
CC       and zygotically.
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   UniGene; Spu.6724; -.
DR   ProteinModelPortal; P10079; -.
DR   SMR; P10079; -.
DR   PRIDE; P10079; -.
DR   GeneID; 373313; -.
DR   KEGG; spu:373313; -.
DR   CTD; 373313; -.
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: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; 19.
DR   Pfam; PF12661; hEGF; 2.
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; Complete proteome; Cytoplasmic vesicle;
KW   Disulfide bond; EGF-like domain; Extracellular matrix; Glycoprotein;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   CHAIN        20   1064       Fibropellin-1.
FT                                /FTId=PRO_0000002732.
FT   DOMAIN       20     55       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN       62    175       CUB. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      176    212       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      214    250       EGF-like 3; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      252    288       EGF-like 4; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      290    326       EGF-like 5; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      328    364       EGF-like 6; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      366    402       EGF-like 7; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      404    440       EGF-like 8; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      442    478       EGF-like 9; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      480    516       EGF-like 10; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      518    554       EGF-like 11; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      556    592       EGF-like 12; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      594    630       EGF-like 13; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      632    668       EGF-like 14; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      670    706       EGF-like 15; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      708    744       EGF-like 16; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      746    782       EGF-like 17; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      784    820       EGF-like 18; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      822    858       EGF-like 19; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      860    896       EGF-like 20. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      898    934       EGF-like 21; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      937   1056       Avidin-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00656}.
FT   CARBOHYD     30     30       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    136    136       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    851    851       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     23     34       {ECO:0000250}.
FT   DISULFID     28     43       {ECO:0000250}.
FT   DISULFID     45     54       {ECO:0000250}.
FT   DISULFID     62     88       {ECO:0000250}.
FT   DISULFID    180    191       {ECO:0000250}.
FT   DISULFID    185    200       {ECO:0000250}.
FT   DISULFID    202    211       {ECO:0000250}.
FT   DISULFID    218    229       {ECO:0000250}.
FT   DISULFID    223    238       {ECO:0000250}.
FT   DISULFID    240    249       {ECO:0000250}.
FT   DISULFID    256    267       {ECO:0000250}.
FT   DISULFID    261    276       {ECO:0000250}.
FT   DISULFID    278    287       {ECO:0000250}.
FT   DISULFID    294    305       {ECO:0000250}.
FT   DISULFID    299    314       {ECO:0000250}.
FT   DISULFID    316    325       {ECO:0000250}.
FT   DISULFID    332    343       {ECO:0000250}.
FT   DISULFID    337    352       {ECO:0000250}.
FT   DISULFID    354    363       {ECO:0000250}.
FT   DISULFID    370    381       {ECO:0000250}.
FT   DISULFID    375    390       {ECO:0000250}.
FT   DISULFID    392    401       {ECO:0000250}.
FT   DISULFID    408    419       {ECO:0000250}.
FT   DISULFID    413    428       {ECO:0000250}.
FT   DISULFID    430    439       {ECO:0000250}.
FT   DISULFID    446    457       {ECO:0000250}.
FT   DISULFID    451    466       {ECO:0000250}.
FT   DISULFID    468    477       {ECO:0000250}.
FT   DISULFID    484    495       {ECO:0000250}.
FT   DISULFID    489    504       {ECO:0000250}.
FT   DISULFID    506    515       {ECO:0000250}.
FT   DISULFID    522    533       {ECO:0000250}.
FT   DISULFID    527    542       {ECO:0000250}.
FT   DISULFID    544    553       {ECO:0000250}.
FT   DISULFID    560    571       {ECO:0000250}.
FT   DISULFID    565    580       {ECO:0000250}.
FT   DISULFID    582    591       {ECO:0000250}.
FT   DISULFID    598    609       {ECO:0000250}.
FT   DISULFID    603    618       {ECO:0000250}.
FT   DISULFID    620    629       {ECO:0000250}.
FT   DISULFID    636    647       {ECO:0000250}.
FT   DISULFID    641    656       {ECO:0000250}.
FT   DISULFID    658    667       {ECO:0000250}.
FT   DISULFID    674    685       {ECO:0000250}.
FT   DISULFID    679    694       {ECO:0000250}.
FT   DISULFID    696    705       {ECO:0000250}.
FT   DISULFID    712    723       {ECO:0000250}.
FT   DISULFID    717    732       {ECO:0000250}.
FT   DISULFID    734    743       {ECO:0000250}.
FT   DISULFID    750    761       {ECO:0000250}.
FT   DISULFID    755    770       {ECO:0000250}.
FT   DISULFID    772    781       {ECO:0000250}.
FT   DISULFID    788    799       {ECO:0000250}.
FT   DISULFID    793    808       {ECO:0000250}.
FT   DISULFID    810    819       {ECO:0000250}.
FT   DISULFID    826    837       {ECO:0000250}.
FT   DISULFID    831    846       {ECO:0000250}.
FT   DISULFID    848    857       {ECO:0000250}.
FT   DISULFID    864    875       {ECO:0000250}.
FT   DISULFID    869    884       {ECO:0000250}.
FT   DISULFID    886    895       {ECO:0000250}.
FT   DISULFID    902    913       {ECO:0000250}.
FT   DISULFID    907    922       {ECO:0000250}.
FT   DISULFID    924    933       {ECO:0000250}.
FT   VAR_SEQ     477    780       Missing (in isoform Ib). {ECO:0000305}.
FT                                /FTId=VSP_000451.
FT   CONFLICT    279    279       L -> S (in Ref. 2; AAA30050).
FT                                {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
//
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