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Database: UniProt
Entry: P98069
LinkDB: P98069
Original site: P98069 
ID   BMPH_STRPU              Reviewed;         639 AA.
AC   P98069;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   10-APR-2019, entry version 117.
DE   RecName: Full=Bone morphogenetic protein 1 homolog;
DE            EC=3.4.24.-;
DE   AltName: Full=SUBMP;
DE   Flags: Precursor;
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 [MRNA].
RC   TISSUE=Embryo;
RX   PubMed=8162855;
RA   Hwang S.P.L., Partin J.S., Lennarz W.J.;
RT   "Characterization of a homolog of human bone morphogenetic protein 1
RT   in the embryo of the sea urchin, Strongylocentrotus purpuratus.";
RL   Development 120:559-568(1994).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU01211};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU01211};
CC   -!- TISSUE SPECIFICITY: Ectodermal and primary mesenchyme cells in
CC       hatched blastula.
CC   -!- DEVELOPMENTAL STAGE: Embryo; highest level before spiculogenesis.
DR   EMBL; L23838; AAA30081.1; -; mRNA.
DR   RefSeq; NP_999728.1; NM_214563.1.
DR   UniGene; Spu.30412; -.
DR   ProteinModelPortal; P98069; -.
DR   SMR; P98069; -.
DR   STRING; 7668.SPU_007317-tr; -.
DR   PRIDE; P98069; -.
DR   GeneID; 373360; -.
DR   KEGG; spu:373360; -.
DR   CTD; 649; -.
DR   eggNOG; KOG3714; Eukaryota.
DR   eggNOG; ENOG410ZPX7; LUCA.
DR   KO; K05502; -.
DR   OrthoDB; 170905at2759; -.
DR   Proteomes; UP000007110; Unassembled WGS sequence.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
DR   CDD; cd00041; CUB; 2.
DR   CDD; cd04281; ZnMc_BMP1_TLD; 1.
DR   Gene3D; 2.60.120.290; -; 2.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR015446; BMP_1/tolloid-like.
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; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001506; Peptidase_M12A.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   InterPro; IPR034036; ZnMP_TLD/BMP1.
DR   Pfam; PF01400; Astacin; 1.
DR   Pfam; PF00431; CUB; 2.
DR   PIRSF; PIRSF001199; BMP_1/tolloid-like; 1.
DR   PRINTS; PR00480; ASTACIN.
DR   SMART; SM00042; CUB; 2.
DR   SMART; SM00181; EGF; 1.
DR   SMART; SM00179; EGF_CA; 1.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF49854; SSF49854; 2.
DR   PROSITE; PS51864; ASTACIN; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS01180; CUB; 2.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Cleavage on pair of basic residues; Complete proteome;
KW   Developmental protein; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Reference proteome; Repeat; Signal; Zinc.
FT   SIGNAL        1     23       {ECO:0000255}.
FT   PROPEP       24    109       {ECO:0000255}.
FT                                /FTId=PRO_0000028895.
FT   CHAIN       110    639       Bone morphogenetic protein 1 homolog.
FT                                /FTId=PRO_0000028896.
FT   DOMAIN      100    305       Peptidase M12A. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01211}.
FT   DOMAIN      307    419       CUB 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      420    531       CUB 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      532    573       EGF-like; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   ACT_SITE    198    198       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   METAL       197    197       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   METAL       201    201       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   METAL       207    207       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   CARBOHYD    122    122       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    140    140       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    317    317       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    455    455       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    143    304       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   DISULFID    167    189       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   DISULFID    169    170       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   DISULFID    307    333       {ECO:0000250}.
FT   DISULFID    360    382       {ECO:0000250}.
FT   DISULFID    420    446       {ECO:0000250}.
FT   DISULFID    473    495       {ECO:0000250}.
FT   DISULFID    536    548       {ECO:0000250}.
FT   DISULFID    544    557       {ECO:0000250}.
FT   DISULFID    559    572       {ECO:0000250}.
SQ   SEQUENCE   639 AA;  71894 MW;  59307B265B7894AD CRC64;
     MDLLYYMTVS LLGFILSLTT FIGETTRALS DDVSSPCKAS GFLGDIALTE DDYEREMIRA
     RHNREQYRRR ILQERQTRTT GARHHIKKRT IEEAKVRHVR AVTARPERRW TDAVIPYEID
     GNFTGSQRAM FKQAMRHWEN YTCITFVERN PANSEHDNHI VFTYQACGCC SFVGRKGDGA
     QAVSVGKNCD KFGVVVHELG HVVGFWHEHT RPDRNEFVGI VHQNIVPGQE YNFRVLDAAE
     VDSLGETYDF ASIMHYARNT FSRGIWLDTI LPRKDPESGI RPEIGQRKHL SEGDIIQANL
     LYKCPSCGRT LLESTGNFSS PEWPGQYDGD QTCVWRISVT PGETISLQFT GFELVGSDGC
     WYNYLEVRDG HWRHSPLLGR FCGASLPDPI LSSDSRLWIE LKSSAHRYSR GFAANYEAIC
     GGHIERESGT LQSPNYPDDY HPSKECVWLI TMPANYTVGL SFQSFEIERH ETCIYDYVEV
     RDGHEDTSPL IGRYCGYFIP DDIKSTGNKM MVTFVSDGSV NKGGFSADFF KEKDECAQPD
     QGGCMDVCVN TIGSYRCDCR PGYELSSDGR RCEVAAEVYS LVYEGISPAL LIPSPIRGTR
     TVSGRSSHHL TTGSHSSLSP LTSRVTRCAS TTTLMSVAV
//
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