BMPH_STRPU
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 03-AUG-2022, entry version 128.
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; Echinoidea;
OC Euechinoidea; Echinacea; Camarodonta; Echinidea; Strongylocentrotidae;
OC Strongylocentrotus.
OX NCBI_TaxID=7668;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=8162855; DOI=10.1242/dev.120.3.559;
RA Hwang S.P.L., Partin J.S., Lennarz W.J.;
RT "Characterization of a homolog of human bone morphogenetic protein 1 in the
RT 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 hatched
CC blastula.
CC -!- DEVELOPMENTAL STAGE: Embryo; highest level before spiculogenesis.
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DR EMBL; L23838; AAA30081.1; -; mRNA.
DR RefSeq; NP_999728.1; NM_214563.1.
DR AlphaFoldDB; P98069; -.
DR SMR; P98069; -.
DR STRING; 7668.SPU_007317-tr; -.
DR MEROPS; M12.016; -.
DR EnsemblMetazoa; NM_214563; NP_999728; GeneID_373360.
DR GeneID; 373360; -.
DR KEGG; spu:373360; -.
DR CTD; 649; -.
DR eggNOG; KOG3714; Eukaryota.
DR OrthoDB; 170905at2759; -.
DR Proteomes; UP000007110; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IBA:GO_Central.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
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; 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; Developmental protein;
KW Disulfide bond; EGF-like domain; Glycoprotein; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Repeat; Signal; Zinc.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..109
FT /evidence="ECO:0000255"
FT /id="PRO_0000028895"
FT CHAIN 110..639
FT /note="Bone morphogenetic protein 1 homolog"
FT /id="PRO_0000028896"
FT DOMAIN 100..305
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 307..419
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 420..531
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 532..573
FT /note="EGF-like; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT ACT_SITE 198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 143..304
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 167..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 169..170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 307..333
FT /evidence="ECO:0000250"
FT DISULFID 360..382
FT /evidence="ECO:0000250"
FT DISULFID 420..446
FT /evidence="ECO:0000250"
FT DISULFID 473..495
FT /evidence="ECO:0000250"
FT DISULFID 536..548
FT /evidence="ECO:0000250"
FT DISULFID 544..557
FT /evidence="ECO:0000250"
FT DISULFID 559..572
FT /evidence="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
