ID A0A423T0M0_PENVA Unreviewed; 899 AA.
AC A0A423T0M0;
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 {ECO:0000313|EMBL:ROT70039.1};
GN ORFNames=C7M84_011717 {ECO:0000313|EMBL:ROT70039.1};
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:ROT70039.1, ECO:0000313|Proteomes:UP000283509};
RN [1] {ECO:0000313|EMBL:ROT70039.1, ECO:0000313|Proteomes:UP000283509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT70039.1};
RA Zhang X., Yuan J., Li F., Xiang J.;
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ROT70039.1, ECO:0000313|Proteomes:UP000283509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT70039.1};
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:ROT70039.1}.
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DR EMBL; QCYY01002482; ROT70039.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423T0M0; -.
DR STRING; 6689.A0A423T0M0; -.
DR Proteomes; UP000283509; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProt.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 6.
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; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR PANTHER; PTHR11640:SF164; MAM DOMAIN-CONTAINING GLYCOSYLPHOSPHATIDYLINOSITOL ANCHOR PROTEIN 1; 1.
DR PANTHER; PTHR11640; NEPHRIN; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF13895; Ig_2; 1.
DR Pfam; PF13927; Ig_3; 2.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 5.
DR SMART; SM00406; IGv; 2.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 5.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000283509};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 629..653
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 33..111
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 117..222
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 227..306
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 311..394
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 404..505
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 515..608
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 680..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..711
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..870
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 899 AA; 99124 MW; DEE7DAED589704F3 CRC64;
MVNCYALNQA LGSTKIDTEV ISVLRECRWG KTPETPVILG YERGQELRKG DRQRLTCVSN
GGNPLATLTW YKGSQKLPSE THHDAVTALA DVDILLDESD NGAEYRCEAT NEATAHPLAN
STVLSFLLQR SRSEPRVINA GSPMTLFCES ASSNPFANIT WWRDGFEVDG EYTVETKPGQ
FGGTVTNYSV KVEVTADDDG AVYTCQADNG FGSTTHDAVT ISVHYSPVWV KEPPKSLDVK
EGENVMLNAS ARGNPNSLAY LWRRGEEVVM ADNILNISGI TRDQAGVYSL DVSNTEGNIF
RNVSINVKYA PIITEVTGSS NVSEGDSVTL VCHVDAVPNP DIEWRREGYN FERTKTKKHA
TRNIAEMTIT NVTKEDTGVF ACHSKNEIGE ATIVNATVIV KHKPIIKTRP QYQKAAAEAG
GNVQMVCRAR GAPYIDFTWY TSENTPIEKA IYSRFTNRYK VEDRKLIDGL VTYESVLHIN
NVTSKDYGFF QCQARNSIGS SHTVIHLDGT SRPDTPLDLK VLNFTHDSVD LEWTPGFDGG
LPQKYRIRYN IDTTKRYQYM DVYPENSTVF TVTGLALGTT YAFSVLSYND KGESGFTDTD
VKATTLRIAP PQERPVEGSK VPTGRVSGII VITITLVGIA LLILNVALVA CFIKRRRLQA
SSDKGSSKST TIEMYAPSSY TGTVTGETLS SISEKSRESY EHEDSTDEYE AEASRANATS
TYLIEQLEPP SQYATRPPPH ILPPPPSHND LNIEDGYDEM IRNQYNIDPT GGYGTLGRRN
PAPDHYNINP ADSHYPPPTH RYNTYQPPTQ HILTAHSHAQ NNGSLRRNPP SKLHFPKDYI
RNGSMNLPGG TGGAGTVGSQ YSNKPQSPTR THAPMLSTFA PEPQQITAGI PLEHRGHLV
//
