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Database: UniProt
Entry: A0A452HEJ9_9SAUR
LinkDB: A0A452HEJ9_9SAUR
Original site: A0A452HEJ9_9SAUR 
ID   A0A452HEJ9_9SAUR        Unreviewed;       287 AA.
AC   A0A452HEJ9;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=ZP domain-containing protein {ECO:0000259|PROSITE:PS51034};
OS   Gopherus agassizii (Agassiz's desert tortoise).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Testudinoidea; Testudinidae; Gopherus.
OX   NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000013243.1, ECO:0000313|Proteomes:UP000291020};
RN   [1] {ECO:0000313|Proteomes:UP000291020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=28562605;
RA   Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA   Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT   "The Agassiz's desert tortoise genome provides a resource for the
RT   conservation of a threatened species.";
RL   PLoS ONE 12:e0177708-e0177708(2017).
RN   [2] {ECO:0000313|Ensembl:ENSGAGP00000013243.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC       protein {ECO:0000256|ARBA:ARBA00004479}. Zona pellucida
CC       {ECO:0000256|ARBA:ARBA00024183}.
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DR   AlphaFoldDB; A0A452HEJ9; -.
DR   STRING; 38772.ENSGAGP00000013243; -.
DR   Ensembl; ENSGAGT00000015160.1; ENSGAGP00000013243.1; ENSGAGG00000010141.1.
DR   Proteomes; UP000291020; Unassembled WGS sequence.
DR   GO; GO:0035805; C:egg coat; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.4100; Zona pellucida, ZP-C domain; 1.
DR   Gene3D; 2.60.40.3210; Zona pellucida, ZP-N domain; 1.
DR   InterPro; IPR042235; ZP-C.
DR   InterPro; IPR001507; ZP_dom.
DR   InterPro; IPR017977; ZP_dom_CS.
DR   PANTHER; PTHR23343; ZONA PELLUCIDA SPERM-BINDING PROTEIN; 1.
DR   PANTHER; PTHR23343:SF41; ZONA PELLUCIDA SPERM-BINDING PROTEIN 1; 1.
DR   Pfam; PF00100; Zona_pellucida; 1.
DR   SMART; SM00241; ZP; 1.
DR   PROSITE; PS00682; ZP_1; 1.
DR   PROSITE; PS51034; ZP_2; 1.
PE   4: Predicted;
KW   Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW   Fertilization {ECO:0000256|ARBA:ARBA00023279};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|ARBA:ARBA00022989};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          1..236
FT                   /note="ZP"
FT                   /evidence="ECO:0000259|PROSITE:PS51034"
FT   REGION          239..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        249..264
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        271..287
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   287 AA;  32004 MW;  91D8983E0AEC340C CRC64;
     MFDHPIILDS VRLAYAQTGC DPIRMIEAFV IFRFPVMQCG ITVQVIGDKL IYENQLISGT
     DVHTRPDGSI TRDSTFILHA CCIYNASGFL PVQAGPLRLG LRIATDRIYR SYLTERDYPV
     VKVLRDPIYV EVHILQRTDP NMVLSLHYCW ATPSANPLEQ PQWPILVDGC PFLGDNYRTQ
     LVPIGSELPF PTHHQRFVLS TFAFVDSASQ IALDGEIRML HCTGTSSQAA IILHEHSTEV
     PTQIGPPPPQ QKHTSSQALT CTVPPPSQEA HARLTPTSNK DAQISYC
//
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