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Database: UniProt
Entry: A0A423TUX2_PENVA
LinkDB: A0A423TUX2_PENVA
Original site: A0A423TUX2_PENVA 
ID   A0A423TUX2_PENVA        Unreviewed;       581 AA.
AC   A0A423TUX2;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=Putative nephrin-like protein {ECO:0000313|EMBL:ROT80251.1};
GN   ORFNames=C7M84_001018 {ECO:0000313|EMBL:ROT80251.1};
OS   Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC   Penaeoidea; Penaeidae; Penaeus.
OX   NCBI_TaxID=6689 {ECO:0000313|EMBL:ROT80251.1, ECO:0000313|Proteomes:UP000283509};
RN   [1] {ECO:0000313|EMBL:ROT80251.1, ECO:0000313|Proteomes:UP000283509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Muscle {ECO:0000313|EMBL:ROT80251.1};
RA   Zhang X., Yuan J., Li F., Xiang J.;
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ROT80251.1, ECO:0000313|Proteomes:UP000283509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Muscle {ECO:0000313|EMBL:ROT80251.1};
RA   Sun Y., Gao Y., Yu Y.;
RT   "The decoding of complex shrimp genome reveals the adaptation for benthos
RT   swimmer, frequently molting mechanism and breeding impact on genome.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ROT80251.1}.
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DR   EMBL; QCYY01001138; ROT80251.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A423TUX2; -.
DR   STRING; 6689.A0A423TUX2; -.
DR   Proteomes; UP000283509; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   CDD; cd00063; FN3; 1.
DR   CDD; cd00096; Ig; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 5.
DR   InterPro; IPR013162; CD80_C2-set.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   PANTHER; PTHR11640:SF162; LIMBIC SYSTEM-ASSOCIATED MEMBRANE PROTEIN; 1.
DR   PANTHER; PTHR11640; NEPHRIN; 1.
DR   Pfam; PF08205; C2-set_2; 1.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF13927; Ig_3; 2.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM00409; IG; 4.
DR   SMART; SM00408; IGc2; 4.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 4.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS50835; IG_LIKE; 4.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000283509};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        515..539
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          24..106
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          111..197
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          202..283
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          290..385
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          396..487
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
SQ   SEQUENCE   581 AA;  62190 MW;  CE7673A25DB37075 CRC64;
     MCTRREEEAE SASLFSVLSL KLIGRREEAA LSCHTTPSRP RSTITWYSRA GVLQATSTVH
     SQAVFGGTIT RSELTIRATA DDNGRVVTCV AQNGLGSSVN VNITVSVLHG PVWVKVPSGR
     LDFLEGGDLV LTAVAAANPP TVSYSWWRGP EMIIGEGISE DGTGALRLNR IHRNQQGNYS
     VSAHTSRGTA HSDFFINVQY GPEDVVAATR VTLDKGGTTS VICSAKGNPT PNITWTRSND
     NTSVLWWGVG EARLVVERAS KEDTGVYLCK ASNSVTTAPP AVTALVVTQP PTTPKEYQSV
     RGWAAIGGNG YLKCHVTAAP TPTFSWSVNG EAFVPNKSKY FVHHPELTDG VALWISVLEV
     RRVTDRDYTS YTCKAHNTEG EHSLSLTLGP PLPPQAPYNL TATVVTTSAV LSWRHSQPED
     SVQGYTVKYH PVDSKEYKFQ DVPGRGGTAA TIKGLIASTQ YAFAVQAYSE QGRSLYSAPF
     YVTTMRDAVE EAASSSTSTG SSNTGSGTQH RVPRLILIII CLTGAALLIL NIVVVTCFLR
     SERAPSTSFD IATTATTPGS ATCVDLVSSD DGSSVARLII R
//
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