ID A0A498NB89_LABRO Unreviewed; 681 AA.
AC A0A498NB89;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Sushi domain-containing 5 {ECO:0000313|EMBL:RXN26495.1};
GN ORFNames=ROHU_036455 {ECO:0000313|EMBL:RXN26495.1};
OS Labeo rohita (Indian major carp) (Cyprinus rohita).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Labeoninae; Labeonini; Labeo.
OX NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN26495.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN26495.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN26495.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN26495.1};
RA Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA Shah T.M., Rai A., Jena J.K.;
RT "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00302}.
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:RXN26495.1}.
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DR EMBL; QBIY01012241; RXN26495.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498NB89; -.
DR STRING; 84645.A0A498NB89; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005540; F:hyaluronic acid binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR CDD; cd00033; CCP; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR000538; Link_dom.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR PANTHER; PTHR32493; SUSHI DOMAIN-CONTAINING PROTEIN 5; 1.
DR PANTHER; PTHR32493:SF0; SUSHI DOMAIN-CONTAINING PROTEIN 5; 1.
DR Pfam; PF00084; Sushi; 1.
DR Pfam; PF00193; Xlink; 1.
DR SMART; SM00032; CCP; 1.
DR SMART; SM00445; LINK; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 1.
DR PROSITE; PS50963; LINK_2; 1.
DR PROSITE; PS50923; SUSHI; 1.
PE 1: Evidence at protein level;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A498NB89};
KW Reference proteome {ECO:0000313|Proteomes:UP000290572};
KW Signal {ECO:0000256|SAM:SignalP};
KW Sushi {ECO:0000256|PROSITE-ProRule:PRU00302};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..681
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019821484"
FT TRANSMEM 631..653
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 33..125
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 129..190
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT REGION 213..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 681 AA; 73665 MW; A7417D327431B332 CRC64;
MGRACHRELT LLSLLGYLAC LTCADVSPLG RVFLLDLESS KGGQEKGFEA ATHACMVQGA
RVASGADLHH AVLECAFSAC SRGWLSGPSV GTTVCSGVPG SLRPVDVQLE NLTADTERLG
VFCVKDSDTP CGQPPSFPYS HLQGKTGLDL GDELLYACDP GYKLPNGDTA FSLLCDSCGE
WYGLVQHCVK DDPEGHIDYE DKFTDGHLRE EHHISLNPGG TQSTDHEVEE SSPEPEPEPE
PEPEPEPERT VMSEEEKEND EDSTISVTEP PVSQLSQKHM FWFPSEAFHE EKKQPVITSD
SSSVKSPNED ESHTMVKTTD SQSGPDVTTE ERDYPTDPPT DEPASPSAGG TDESWLDGYP
VTQDEDKAGG ESTGEVGSEQ GGESETETLT GHSEVEVFKD VAKNPVEEEE TGGLIDNPEE
EGGEMKNPED TILRKGDEEE FGKGTIRFEK GESVVTPHKE TTEGLAEDET VKETYAPEET
DSKTLGFDDV TDSPAVVEVK PTTFITQTTP SPDDTTVHKW PMPYTPASAP ENVSTSQSGL
GLESTTTPSG MVHLDGIPDF ITSIPTPVIK DPWETFDDHI LEHIPGHVPT ENPENRSVME
RGGDHSLDQQ ERAGEGACAE DPCHGSGRGP MIAAIIIAVV AAVVGAILGV WCYKKRQQKS
SHYQLNGTNR QTQCIELQQT V
//
