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Database: UniProt
Entry: K7FTY9_PELSI
LinkDB: K7FTY9_PELSI
Original site: K7FTY9_PELSI 
ID   K7FTY9_PELSI            Unreviewed;      1227 AA.
AC   K7FTY9;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=Attractin {ECO:0000313|Ensembl:ENSPSIP00000011499.1};
GN   Name=ATRN {ECO:0000313|Ensembl:ENSPSIP00000011499.1};
OS   Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC   Trionychidae; Pelodiscus.
OX   NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000011499.1, ECO:0000313|Proteomes:UP000007267};
RN   [1] {ECO:0000313|Proteomes:UP000007267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG   Soft-shell Turtle Genome Consortium;
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000007267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX   PubMed=23624526; DOI=10.1038/ng.2615;
RA   Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA   White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA   Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA   Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA   Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT   "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT   into the development and evolution of the turtle-specific body plan.";
RL   Nat. Genet. 45:701-706(2013).
RN   [3] {ECO:0000313|Ensembl:ENSPSIP00000011499.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00460}.
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DR   EMBL; AGCU01203117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01203118; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01203119; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01203120; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01203121; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01203122; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01203123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01203124; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01203125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01203126; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; K7FTY9; -.
DR   Ensembl; ENSPSIT00000011556.1; ENSPSIP00000011499.1; ENSPSIG00000010130.1.
DR   GeneTree; ENSGT00940000157346; -.
DR   Proteomes; UP000007267; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd00055; EGF_Lam; 1.
DR   Gene3D; 2.120.10.80; Kelch-type beta propeller; 2.
DR   Gene3D; 2.10.25.10; Laminin; 2.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR006652; Kelch_1.
DR   InterPro; IPR002049; LE_dom.
DR   InterPro; IPR002165; Plexin_repeat.
DR   InterPro; IPR016201; PSI.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   PANTHER; PTHR46376:SF3; ATTRACTIN; 1.
DR   PANTHER; PTHR46376; LEUCINE-ZIPPER-LIKE TRANSCRIPTIONAL REGULATOR 1; 1.
DR   Pfam; PF01344; Kelch_1; 3.
DR   Pfam; PF13964; Kelch_6; 1.
DR   Pfam; PF01437; PSI; 2.
DR   SMART; SM00034; CLECT; 1.
DR   SMART; SM00180; EGF_Lam; 2.
DR   SMART; SM00423; PSI; 5.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF117281; Kelch motif; 1.
DR   SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS01248; EGF_LAM_1; 1.
DR   PROSITE; PS50027; EGF_LAM_2; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00076};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Kelch repeat {ECO:0000256|ARBA:ARBA00022441};
KW   Laminin EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00460};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007267};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        1077..1101
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          44..81
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          593..717
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          861..906
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DISULFID        48..58
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        52..69
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        71..80
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        878..887
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        890..904
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ   SEQUENCE   1227 AA;  136636 MW;  F3F2665FB28BB533 CRC64;
     SGLIVPERDG NETVPEVVTT SGYVLLHFFS DAAYNLTGFN ITYHFDMCPN NCSGRGECKL
     GNGSNTVQCE CSEHWKGEAC DIPYCTDDCG YPERGQCTSN GTKGCSCYSN WQGPGCAIPV
     PANQSFWTRE EHSSPKLPRA SHKAVVNGHV MWVVGGYRFN HSDSHMVLAY DLVSEEWLPL
     NNTVNLVQIR YGHSLALHEN KIYMYGGKID STGNVTNQLW VFHIHNESWV QVTPKAKEQY
     AVVGHSAHIV TLEDGSIVML VIFGHCPLYG YVSNMQEYNL ATNTWNIVRT SGALVQGGYG
     HSSVYDPNSK SIYIHGGYKA FSANKYRLAD DLYKYEVETQ MWTILKDSRF FRYLHTAVIM
     SGTMLVFGGN THNDTSMSHG AKCFSSDFMA YDIACDQWSV LPRPDLHHDV NRFGHSAVLS
     NSTMYVFGGF NSLLLSDILR YTPESCEAYG NETSCFKAGP GIRCVWNTTF SQCVPWEAAT
     VEQQQKVFEE CPSKPVADDE KCRQITDCYS CTANTNSCQW CTDQCILKHS NCTEDQVPII
     EYDKCPKDNP AYYCNKRTSC KSCAMDQNCQ WEPRNQECIA LPENICGANW HLVGNSCLKI
     ASTKESYDNA KLTCRNANAL LASLTTQKKV EFVLKELQKM QSVVSVTPKT LTPWVGLRKI
     NVSYWCWEDM SPFTNTSLQW LPGEPSGAGF CGYLAEPYQQ GLKAATCINQ VNGSVCERPA
     NHSAKQCRTP CALRMMCGEC TSGSSECMWC SNMKQCVDSN AYVASFPYGQ CLEWYTMSSC
     PPENCSGYCT CGHCLEQPGC GWCTDPSNTG KGKCMEGSYR GPVKIPSPST TGKHYMEPIL
     NVSMCPAENK YNWSFIQCPA CQCNGHSKCV NESICEKCEN LTTGKHCETC ISGYYGDPTN
     GGTCQSCKCN GHASICNTNT GKCFCTTKGI KGDECQLCEV ENRYQGNPLK GTCYYTLLID
     YQFTFSLSQE DDRYYTAINF VATPEEQNRD LDMFINASKN FNLNITWSTS FAAGTQAGEE
     IPVISKSNIK EYKDSFSNEK FDFRNNPNIT FFVYVSNFTW PIKIQIAFSQ HSNFMDLVQF
     FVTFFSCFLS LLLVAAVVWK IKQSCWASRR REQLLREMQQ MASRPFASIN VALETDEEPP
     DLIGGSIKTV PKPIALEPCF GNRAAVLSVF VRLPRGLGGI PPPGQSGLAV ASALVDVSQQ
     MPIAYKEKSG AIRNRKQQPP AQPGTCI
//
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