ASTL_CHICK
ID ASTL_CHICK Reviewed; 409 AA.
AC P0DJJ2;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Astacin-like metalloendopeptidase;
DE EC=3.4.-.-;
DE Flags: Precursor;
GN Name=ASTL;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-40.
RX PubMed=16903475; DOI=10.1093/ps/85.8.1438;
RA Froman D.P., Kirby J.D., Rhoads D.D.;
RT "An expressed sequence tag analysis of the chicken reproductive tract
RT transcriptome.";
RL Poult. Sci. 85:1438-1441(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 213-409.
RC STRAIN=White Leghorn Hisex;
RX PubMed=12445392; DOI=10.1016/s0960-9822(02)01296-4;
RA Boardman P.E., Sanz-Ezquerro J., Overton I.M., Burt D.W., Bosch E.,
RA Fong W.T., Tickle C., Brown W.R., Wilson S.A., Hubbard S.J.;
RT "A comprehensive collection of chicken cDNAs.";
RL Curr. Biol. 12:1965-1969(2002).
RN [4]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=22275110; DOI=10.1002/dvdy.23737;
RA Acloque H., Lavial F., Pain B.;
RT "Astacin-like metallo-endopeptidase is dynamically expressed in embryonic
RT stem cells and embryonic epithelium during morphogenesis.";
RL Dev. Dyn. 241:574-582(2012).
CC -!- FUNCTION: Probable oocyte-specific oolemmal receptor involved in sperm
CC and egg adhesion and fertilization. May act as a protease (By
CC similarity). {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6HA09}. Cell
CC membrane {ECO:0000250|UniProtKB:Q6HA09}. Cytoplasmic vesicle, secretory
CC vesicle, Cortical granule {ECO:0000250|UniProtKB:Q6HA09}.
CC -!- TISSUE SPECIFICITY: Expressed in ovary and gonads.
CC {ECO:0000269|PubMed:22275110}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryonic stem cells. Expressed in
CC the pluripotent cells of the epiblast. Detected at the junction of non-
CC neuronal and neuronal ectoderm just before neural tube closure.
CC Expressed in the ventral epidermis before ventral closure, in the
CC intermediate mesoderm, gonads and the forming nephric duct and tubules
CC of the mesonephros and metanephros. {ECO:0000269|PubMed:22275110}.
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DR EMBL; DT656838; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BU266437; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001292019.1; NM_001305090.2.
DR AlphaFoldDB; P0DJJ2; -.
DR SMR; P0DJJ2; -.
DR STRING; 9031.ENSGALP00000013074; -.
DR PaxDb; P0DJJ2; -.
DR Ensembl; ENSGALT00000071502; ENSGALP00000046927; ENSGALG00000037220.
DR GeneID; 423176; -.
DR KEGG; gga:423176; -.
DR CTD; 431705; -.
DR VEuPathDB; HostDB:geneid_423176; -.
DR eggNOG; KOG3714; Eukaryota.
DR GeneTree; ENSGT00940000161051; -.
DR HOGENOM; CLU_005140_1_0_1; -.
DR InParanoid; P0DJJ2; -.
DR OMA; GIHEAMA; -.
DR OrthoDB; 455209at2759; -.
DR PRO; PR:P0DJJ2; -.
DR Proteomes; UP000000539; Chromosome 5.
DR GO; GO:0060473; C:cortical granule; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0070001; F:aspartic-type peptidase activity; ISS:UniProtKB.
DR GO; GO:0070002; F:glutamic-type peptidase activity; ISS:UniProtKB.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0008233; F:peptidase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
DR GO; GO:0009566; P:fertilization; ISS:UniProtKB.
DR GO; GO:2000360; P:negative regulation of binding of sperm to zona pellucida; ISS:UniProtKB.
DR GO; GO:0010954; P:positive regulation of protein processing; ISS:UniProtKB.
DR GO; GO:0060468; P:prevention of polyspermy; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00041; CUB; 1.
DR CDD; cd04283; ZnMc_hatching_enzyme; 1.
DR Gene3D; 2.60.120.290; -; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR017370; Hatching_enzyme_Uvs2-like.
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; IPR034039; ZnMP_hatching_enz.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF00431; CUB; 1.
DR PIRSF; PIRSF038057; Hatching_enzyme_Uvs2; 1.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF49854; SSF49854; 1.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS01180; CUB; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cytoplasm; Cytoplasmic vesicle; Disulfide bond;
KW Fertilization; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Signal; Zinc; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..409
FT /note="Astacin-like metalloendopeptidase"
FT /id="PRO_0000418131"
FT DOMAIN 87..285
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 287..399
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT REGION 30..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 91..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 134..284
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 155..175
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 287..313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 339..362
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
SQ SEQUENCE 409 AA; 46388 MW; A90E0C096E97036C CRC64;
MDLKMLLIFI AFLLPSVLGF PIQDNYENST ATTESTQVTT EEDIYDSPSP AETDSEDELI
FNRILEVNKD SSQYLQEGDI VPRRSRSAIN CRNCYWPQSR DGIVRIPYVL DPTYEENHVK
GIREAMAEFE TLTCINFVKR KTERDYLIIR SADGCWSNYG KVGGGQTISV MKGGCMWKGI
IQHELDHALG FLHEHSRSDR DKYVRIMWEY ISPADRPDFK KFENSNNLGL PYDYSSVMHY
GPHTFTNTTG KATIVPVPDG SVHIGQRLGL SNLDVAKINR LYNCSRCSTI IDAAFGSLKS
ANYPRNYSDN TNCVWLIRTR SRKISLHFRA FELRTTRGCQ GDYVKVYDGS SKYSTVLMDK
TCGSQIPTDV VSSSNLMLIE FVTDGADTAS GFQATFTSAK IQRRFKIRN
