ID   ZPP_ACRMI               Reviewed;         414 AA.
AC   G8HTB6;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   25-JAN-2012, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=ZP domain-containing protein {ECO:0000303|PubMed:23765379};
DE   Flags: Precursor;
OS   Acropora millepora (Staghorn coral) (Heteropora millepora).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC   Astrocoeniina; Acroporidae; Acropora.
OX   NCBI_TaxID=45264;
RN   [1] {ECO:0000312|EMBL:AET09743.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=22065994; DOI=10.1371/journal.pone.0026411;
RA   Hayward D.C., Hetherington S., Behm C.A., Grasso L.C., Foret S.,
RA   Miller D.J., Ball E.E.;
RT   "Differential gene expression at coral settlement and metamorphosis - a
RT   subtractive hybridization study.";
RL   PLoS ONE 6:E26411-E26411(2011).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 142-153; 166-173 AND 214-227, TISSUE SPECIFICITY, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=23765379; DOI=10.1093/molbev/mst109;
RA   Ramos-Silva P., Kaandorp J., Huisman L., Marie B., Zanella-Cleon I.,
RA   Guichard N., Miller D.J., Marin F.;
RT   "The skeletal proteome of the coral Acropora millepora: the evolution of
RT   calcification by co-option and domain shuffling.";
RL   Mol. Biol. Evol. 30:2099-2112(2013).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}. Note=Presence in the organic matrix of the
CC       skeleton may be due to shedding of a soluble peptide. {ECO:0000255,
CC       ECO:0000303|PubMed:23765379}.
CC   -!- TISSUE SPECIFICITY: Component of the acid-insoluble and acid-soluble
CC       organic matrix of the aragonitic skeleton (at protein level).
CC       {ECO:0000269|PubMed:23765379}.
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DR   EMBL; JN631095; AET09743.1; -; mRNA.
DR   AlphaFoldDB; G8HTB6; -.
DR   SMR; G8HTB6; -.
DR   PRIDE; G8HTB6; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.4100; -; 1.
DR   InterPro; IPR042235; ZP-C.
DR   InterPro; IPR001507; ZP_dom.
DR   Pfam; PF00100; Zona_pellucida; 1.
DR   SMART; SM00241; ZP; 1.
DR   PROSITE; PS51034; ZP_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Membrane; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..414
FT                   /note="ZP domain-containing protein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000429754"
FT   TOPO_DOM        18..364
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        365..385
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        386..414
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          70..323
FT                   /note="ZP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT   REGION          18..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        241..302
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   414 AA;  45707 MW;  A1285A33805D73F3 CRC64;
     MFLYSFVFLM LLGLSSAQTE SATSPDEVET EPTMSTDQPE TSPSMSTETE PTTETPPVTT
     PPPPDSLSVI CTNEKMEVFL DHAKHDNLDL DKVTLKDANC KASGTLNATH LWMDVPFDSC
     MTNHSTDGDT ITYQNSLVAE TRASAGSSLI SREFQAEFPF KCTYPRSAVL SVVAFSPRER
     IVYTKTAEFG NFTFTMDMYK TDKYETPYDS FPVRLDLDDP MFLEVKVSSN DSKLVLIPLK
     CWATPSSDLQ DDKYYTFIEN GCGKADDPSL VFNYGESNVQ RFKIGAFRFI GESLNSNVYL
     HCDVEACRKG DSDSRCAKGC ETSRRRRRSS LASSAGTEQT VTLGPMKISE KAEVGAQEAV
     SSLTIFAAVA GVLGVIVLFL AVALVMLYKR YRSPQSATRV VYTKTANEEG KLLV