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Database: UniProt
Entry: P98068
LinkDB: P98068
Original site: P98068 
ID   SPAN_STRPU              Reviewed;         616 AA.
AC   P98068;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   10-APR-2019, entry version 99.
DE   RecName: Full=Protein SpAN;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   Name=SPAN;
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].
RX   PubMed=1618141;
RA   Reynolds S.D., Angerer L.M., Palis J., Nasir A., Angerer R.C.;
RT   "Early mRNAs, spatially restricted along the animal-vegetal axis of
RT   sea urchin embryos, include one encoding a protein related to tolloid
RT   and BMP-1.";
RL   Development 114:769-786(1992).
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: Asymmetrically along the animal-vegetal axis
CC       of the blastula.
CC   -!- DEVELOPMENTAL STAGE: Very early blastula (between 16-cell stage
CC       and hatching).
DR   EMBL; M84144; AAA30072.1; -; mRNA.
DR   RefSeq; NP_999767.1; NM_214602.2.
DR   UniGene; Spu.977; -.
DR   ProteinModelPortal; P98068; -.
DR   SMR; P98068; -.
DR   MEROPS; M12.013; -.
DR   PRIDE; P98068; -.
DR   GeneID; 593517; -.
DR   KEGG; spu:373442; -.
DR   CTD; 20691; -.
DR   eggNOG; KOG3714; Eukaryota.
DR   eggNOG; ENOG410ZPX7; LUCA.
DR   InParanoid; P98068; -.
DR   Proteomes; UP000007110; Unassembled WGS sequence.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
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; cd04280; ZnMc_astacin_like; 1.
DR   Gene3D; 2.60.120.290; -; 2.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR034035; Astacin-like_dom.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001506; Peptidase_M12A.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   InterPro; IPR017369; SPAN/blastula_protease_10.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   Pfam; PF01400; Astacin; 1.
DR   Pfam; PF00431; CUB; 2.
DR   PIRSF; PIRSF038056; BP10_SPAN; 1.
DR   PRINTS; PR00480; ASTACIN.
DR   SMART; SM00042; CUB; 2.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF49854; SSF49854; 2.
DR   PROSITE; PS51864; ASTACIN; 1.
DR   PROSITE; PS01180; CUB; 2.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Complete proteome;
KW   Developmental protein; Disulfide bond; EGF-like domain; Hydrolase;
KW   Metal-binding; Metalloprotease; Protease; Reference proteome; Repeat;
KW   Signal; Zinc.
FT   SIGNAL        1     16       {ECO:0000255}.
FT   PROPEP       17     93       Activation peptide. {ECO:0000255}.
FT                                /FTId=PRO_0000028899.
FT   CHAIN        94    616       Protein SpAN.
FT                                /FTId=PRO_0000028900.
FT   DOMAIN       93    294       Peptidase M12A. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01211}.
FT   DOMAIN      289    329       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      340    450       CUB 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      503    614       CUB 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   COMPBIAS     89     93       Arg/Lys-rich (basic).
FT   COMPBIAS    451    502       Thr-rich.
FT   ACT_SITE    191    191       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   METAL       190    190       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   METAL       194    194       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   METAL       200    200       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   DISULFID    134    293       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   DISULFID    162    182       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   DISULFID    299    317       {ECO:0000250}.
FT   DISULFID    319    328       {ECO:0000250}.
FT   DISULFID    340    366       {ECO:0000250}.
FT   DISULFID    393    413       {ECO:0000250}.
FT   DISULFID    503    529       {ECO:0000250}.
FT   DISULFID    556    576       {ECO:0000250}.
SQ   SEQUENCE   616 AA;  67902 MW;  397CD923FFB9EB98 CRC64;
     MKLVLLLAGF AALAKCSLAA PAGVQKDIPM ETSAPEKPSE ATTLGLLKTP KPEPKDEEPS
     PGAFQGDMML TDDQLRKVEE AIDDQKAGRK KRKATIYESQ RWSYKIIPYV IESSSSGQSS
     LIRSAMDHWE QNTCLRFEPL TSSHSSRLGH TSYISFFRGN GCWSHVGRSF TNQQQISIGP
     QCGYFGTIVH EIGHAIGFHH EQSRPDRDEY INVHFENVQS GREHNFAKYT WGSVTSSNVE
     YDVGSIMHYG GYGFSSNGRP TITTIDPRLN SRLGQRTALS AADIELANRI YECDDVEDCS
     NADECLNGGY HDADCDCVCP SSYSGDLCQD GGPTVRPADC SYRFTEMTGE ITSPNYPSNY
     EDNTACVYEI EGPYGSTIEL TFLDMEIETE TLCRYDAVEV RKDDINSIGE KFCGNTLPPV
     QISSSNQMMV SFTSDPSITR RGFKATYVII IQTTTVFSTT TLQTTPPSTT TLQTTNPSTT
     TLQTTNPSTT TLQTTDTPVI GSCGGTFVGV EGRVASPNYP NDYDNSLQCD YVIEVDDGRR
     VELIFEDFGL EDETTCRWDS LMINLGNGIK VGMKMCGREY PAASLVSIGN RMELKLKTDG
     SVNDRGFVAS YRAIDL
//
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