ID A0A498NG59_LABRO Unreviewed; 1238 AA.
AC A0A498NG59;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Kringle-containing protein marking the eye and the nose {ECO:0000256|ARBA:ARBA00032328};
GN ORFNames=ROHU_017488 {ECO:0000313|EMBL:RXN30818.1};
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:RXN30818.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN30818.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN30818.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN30818.1};
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00121}.
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:RXN30818.1}.
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DR EMBL; QBIY01011545; RXN30818.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498NG59; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd00033; CCP; 1.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00108; KR; 1.
DR Gene3D; 4.10.410.20; -; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 1.
DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 1.
DR InterPro; IPR005533; AMOP_dom.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR018056; Kringle_CS.
DR InterPro; IPR038178; Kringle_sf.
DR InterPro; IPR036024; Somatomedin_B-like_dom_sf.
DR InterPro; IPR001212; Somatomedin_B_dom.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR InterPro; IPR001846; VWF_type-D.
DR InterPro; IPR002889; WSC_carb-bd.
DR PANTHER; PTHR13802; MUCIN 4-RELATED; 1.
DR PANTHER; PTHR13802:SF63; SUSHI DOMAIN-CONTAINING PROTEIN 2; 1.
DR Pfam; PF03782; AMOP; 1.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF00051; Kringle; 1.
DR Pfam; PF01033; Somatomedin_B; 1.
DR Pfam; PF00084; Sushi; 1.
DR Pfam; PF00094; VWD; 1.
DR Pfam; PF01822; WSC; 1.
DR PRINTS; PR00018; KRINGLE.
DR SMART; SM00723; AMOP; 1.
DR SMART; SM00032; CCP; 1.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00130; KR; 1.
DR SMART; SM00201; SO; 1.
DR SMART; SM00216; VWD; 1.
DR SMART; SM00321; WSC; 1.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 1.
DR SUPFAM; SSF57440; Kringle-like; 1.
DR SUPFAM; SSF90188; Somatomedin B domain; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR PROSITE; PS50856; AMOP; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS00021; KRINGLE_1; 1.
DR PROSITE; PS50070; KRINGLE_2; 1.
DR PROSITE; PS00524; SMB_1; 1.
DR PROSITE; PS50958; SMB_2; 1.
DR PROSITE; PS50923; SUSHI; 1.
DR PROSITE; PS51233; VWFD; 1.
DR PROSITE; PS51212; WSC; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00302};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121}; Membrane {ECO:0000256|SAM:Phobius};
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};
KW Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1238
FT /note="Kringle-containing protein marking the eye and the
FT nose"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019856257"
FT TRANSMEM 780..805
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1032..1055
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1160..1182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 26..67
FT /note="SMB"
FT /evidence="ECO:0000259|PROSITE:PS50958"
FT DOMAIN 281..429
FT /note="AMOP"
FT /evidence="ECO:0000259|PROSITE:PS50856"
FT DOMAIN 441..635
FT /note="VWFD"
FT /evidence="ECO:0000259|PROSITE:PS51233"
FT DOMAIN 721..778
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 824..907
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 909..1003
FT /note="WSC"
FT /evidence="ECO:0000259|PROSITE:PS51212"
FT DOMAIN 1007..1096
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT REGION 1108..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 749..776
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 1238 AA; 137360 MW; B9121544764E61F1 CRC64;
MLCKYKDKIH LCMFIVLLLQ LLSRTAAQSC ANSCGEKLNT CSCHATCESL KDCCADYKQF
CLDIEPYSGS LLGGRDFKIL NATFEQNINL TCRFNSEILT EGYVDESGVG HCISPLLYES
GWIPFEVSTD GVNYDRAGRW LSVHHSKLSP FYTIVMVNAT QWQYYGTPNV SGDLKMIWIP
SLIKAETVNV ELWGYNETGE AYSANWEAEW KYLYTVTRDV PNVGTFVFTP QIAEKPYSLW
DLGSMRIIPS TKPDGAQNVN ALWSGAHAIA WHLEEAFRMD SAGWALEKCI NWDKEEKAMP
SFQTEIIDCP CTLAQARADT GRFHTDYGCD IEAGSFCVYH PGAVHCVRAI QGSPEYGAGQ
QCCYDSTGAQ VLTGDSIGGS TPDRGHDWGD PPYKKPPRVP GFSHWKYDVI SFYYCCLWSD
NCEYYFTHRP SSDCRTYHPP RTAAVLGDPH FMTFDGVTFT FNGKGEYSLV HSPHYDLSVQ
GRTEPMKFEN GTVAMATRLS SVAMREKDSD IIEVRLGDQV DELKVLMNQQ VLSFSEQKWI
DLKGVFVFSP NPTNVTVMFP SGTGVEVRAG QGVMTLTVLL PHNLQNHTQG LLGTMNDDPE
DDFTSSSGVI IPLNSSAQDI FTYCAGWAIT NETSLFTYDS TYLLYEYYYA PKHDPSFIPN
FSVTEDPEDP LLEPTLNLCA GEGASFCKYD ALSMRSLEQG NATLLAYRSH TATRKALAPV
QSCGWLSPPN HGQKEGTLYL EGATVDFSCN DGYRLYGSQE RTCQADGTWT GRDTHCVADF
TLAIVLGSVG AVLALVVMVI AIVVYTKKQK KAIGFLDSPQ RATECYTANG EDYRGRQNQT
SLEGGRPCLF WNETFQHPYN TNKYPNGEGG LGPHNFCRNP DGDVRPWCYI ADLEDGIYWK
YCDIPSCQMP GNLGCFKDNG DPTPLSGGYQ TSNKLTIQNC ISFCRNQRYK LAGMESGYAC
FCGNDLDYHR HGDAPSTECN HVCFGDHTQP CGGDGRVIVF DTKVGACGGN YTSTSAVIYS
PDFPDKYRPG RVCYWTIQVP GASVILFNFT FFNIVDQTDM VELLDGYSNQ VVARFDGRNP
PRDIVNITAD FLIATYYFPT ALRNQAVTPV EGDDDGDEED TSTMRPHTGS TTAKSNTSQN
GKSPLRYYVI TSSPANMPVW TIYALAALLT LTVIAMVAKL LLHLTVKSPS IPSISGSDSC
AQSTTSEPWI IFYRPSTISL FKKKLKNHHG DLSPLVGN
//
