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 27-MAR-2024, entry version 115.
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; Echinoidea;
OC Euechinoidea; Echinacea; Camarodonta; Echinidea; Strongylocentrotidae;
OC Strongylocentrotus.
OX NCBI_TaxID=7668;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1618141; DOI=10.1242/dev.114.3.769;
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 sea
RT urchin embryos, include one encoding a protein related to tolloid and BMP-
RT 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 of the
CC blastula.
CC -!- DEVELOPMENTAL STAGE: Very early blastula (between 16-cell stage and
CC hatching).
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DR EMBL; M84144; AAA30072.1; -; mRNA.
DR RefSeq; NP_999767.1; NM_214602.2.
DR AlphaFoldDB; P98068; -.
DR SMR; P98068; -.
DR MEROPS; M12.013; -.
DR GeneID; 593517; -.
DR KEGG; spu:593517; -.
DR CTD; 20691; -.
DR eggNOG; KOG3714; Eukaryota.
DR HOGENOM; CLU_464090_0_0_1; -.
DR InParanoid; P98068; -.
DR OrthoDB; 2874123at2759; -.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd04280; ZnMc_astacin_like; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR InterPro; IPR034035; Astacin-like_dom.
DR InterPro; IPR000859; CUB_dom.
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 PANTHER; PTHR10127:SF887; ASTACIN-LIKE METALLOENDOPEPTIDASE; 1.
DR PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
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; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 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; Developmental protein; Disulfide bond;
KW EGF-like domain; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Repeat; Signal; Zinc.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..93
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000028899"
FT CHAIN 94..616
FT /note="Protein SpAN"
FT /id="PRO_0000028900"
FT DOMAIN 93..294
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 289..329
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 340..450
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 503..614
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT REGION 30..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 134..293
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 162..182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 299..317
FT /evidence="ECO:0000250"
FT DISULFID 319..328
FT /evidence="ECO:0000250"
FT DISULFID 340..366
FT /evidence="ECO:0000250"
FT DISULFID 393..413
FT /evidence="ECO:0000250"
FT DISULFID 503..529
FT /evidence="ECO:0000250"
FT DISULFID 556..576
FT /evidence="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
//
