ID A0A498M3U2_LABRO Unreviewed; 1737 AA.
AC A0A498M3U2;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=FH2 domain-containing 1 {ECO:0000313|EMBL:RXN12325.1};
GN ORFNames=ROHU_037275 {ECO:0000313|EMBL:RXN12325.1};
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:RXN12325.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN12325.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN12325.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN12325.1};
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:PRU00090}.
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:RXN12325.1}.
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DR EMBL; QBIY01013072; RXN12325.1; -; Genomic_DNA.
DR STRING; 84645.A0A498M3U2; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0019904; F:protein domain specific binding; IEA:InterPro.
DR CDD; cd07660; BAR_Arfaptin; 1.
DR CDD; cd07446; CRD_SFRP2; 1.
DR CDD; cd03580; NTR_Sfrp1_like; 1.
DR Gene3D; 2.40.50.120; -; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR010504; AH_dom.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR027649; Inf2.
DR InterPro; IPR001134; Netrin_domain.
DR InterPro; IPR018933; Netrin_module_non-TIMP.
DR InterPro; IPR041764; SFRP2_CRD.
DR InterPro; IPR008993; TIMP-like_OB-fold.
DR PANTHER; PTHR46345:SF4; FORMIN-J-LIKE; 1.
DR PANTHER; PTHR46345; INVERTED FORMIN-2; 1.
DR Pfam; PF06456; Arfaptin; 1.
DR Pfam; PF02181; FH2; 1.
DR Pfam; PF01392; Fz; 1.
DR SMART; SM01015; Arfaptin; 1.
DR SMART; SM00643; C345C; 1.
DR SMART; SM00498; FH2; 1.
DR SMART; SM00063; FRI; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR SUPFAM; SSF63501; Frizzled cysteine-rich domain; 1.
DR SUPFAM; SSF50242; TIMP-like; 1.
DR PROSITE; PS50870; AH; 1.
DR PROSITE; PS51444; FH2; 1.
DR PROSITE; PS50038; FZ; 1.
DR PROSITE; PS50189; NTR; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00090}; Reference proteome {ECO:0000313|Proteomes:UP000290572};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1737
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019837784"
FT DOMAIN 33..153
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 170..299
FT /note="NTR"
FT /evidence="ECO:0000259|PROSITE:PS50189"
FT DOMAIN 465..634
FT /note="AH"
FT /evidence="ECO:0000259|PROSITE:PS50870"
FT DOMAIN 668..1048
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT REGION 280..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1109..1132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1265..1325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1413..1737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 602..633
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 282..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1109..1131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1283..1304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1305..1323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1442..1495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1500..1537
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1590..1673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1688..1737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 48..94
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 85..123
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 116..140
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 1737 AA; 193218 MW; 287B0E1744CE47FD CRC64;
MMLAYLALLV ALCLPGYLDA LHGFAFDQPE LFQKKSNCKP IPANLLLCHD IEYTDMRLPN
LLGHETMNEV LQQASSWTPL VQKQCHKDTK KFLCSLFAPV CLDDVDEPIQ PCRSLCESVK
SGCAPVMAAF GFPWPDMLNC SRFPLDNDLC IPPAGADALV PVTKEVPRVC EACKEKPEND
NEIVDSLCKN DFALKIKVKE ISYMNGDTKI IPETKSKTIY KLNGGVTDRD FRKIVLWLKD
GLQCVCDEMN DINAAYLVMG QKMDGNLVIT SLKRWQKGMS EASFDSGKNA SQDNQSDPNE
QGHQNTADSV AMAEEAHRSP AAQISVTRNG EADKSHDEVF HRDVPHNISS GPIASHSHNS
PENYAVNEGV VQVGQYSGSP FQATTPKVVP SPAAASRLAR SISDSQVETR KGALREQQTG
GAVVLADDMK SPAIEKLELV KKWSINTYKC TKQILSEKLG RGSRTVDLEL EAQIEVLRDN
KRKYEHVIKL AQTLCTQLAQ MLQTQRQLGD AFADLSLKTP ELHEEFGYNA ETQKLLAKNG
ETLLGAINFF ISNVKTLVDK TIEDTLINIK QYEAARIEYD AYRTDLEELN LGPRDANTLP
KIELSQQQFQ IHREKYEKMR NDVSVKLKFL EENKLGFQHS VTFVNVMTVI IVNRFGAAYL
GVLLYAVADI AAKTPLSSKG LTSHRTTVGK ILEATARHYG SSLVQLLVQL EGFFQIFQII
PFLFSVHPVS LCSVCMISIL DSKRGMNIGI FLKQFKKSNH AIVEDISLGN SKQYGAEPLK
ELLKLLPEAE EVKRLKEFKG DPNKLTLVDS FMFLLIQVPR FDVRIEAMVL QEEFVPSCAA
MSREINIVRQ ATEELMTCEE LHAILHLVLQ AGNIMNAGGY AGNAVGFKLS SLLSLADTKA
NKPGMNLLHF VALEAEKKDE ALLKFPEKLT HVQSAARISV ENIEGEFSSL YVKTRSLEQK
IQDDDELQKQ LDPFLEALQD LKHRRLDLRK EGNALIDFFC EDKDTFKLDE CFRIFQDFCL
KFKKAVKDNR DRELKEEARQ RRLRELEERR CAWGAANTEA GGFGRSSSEN DVDILTKEGL
LDFLLQSRPQ SPHSPLGRSA SARRYHHTEL ISGSSPSDHT KFSSLPRPTR NHQRKTMAWL
VLQDDNRELG PQSQVYQEKL ATSPKAETEP ISPLARYSNF GHNMNNDPYN NNNYSSLSEG
GVTPQLSNPK HVFQGTPGQN VGHMNVSVEK HKLVTGLQPF EITSQINNNS HVSMDNQNVF
VTDLEREEDS PRAFVLDTPP SSRSSEERPK PEKVWNDTRI SSQREEADTS TFSSTTCDTP
LPLDPSMSSK KPALYVMDCT ETDCSIVLDC SEIESSPIIK EKSELKSQDA SFPRVIQDTN
SLSSNFESTD CHFVSTSGEE LIAGRVNQAC PESFSPSVTT EEAETDSCDT AEGRKVGEKA
VQTGSPKTTL VKARTSSKVT AHASRPTRTL TPTETQNMRK VVPITRQNRS SSSMRKVEKP
AGYENTEPRR PLRDQSMPAR RGERQGRPAR HSSLPPEDPR VQRGATPSNS RWSRDLTQHR
PSIKKTNSRP VRNISKPAPE EKMCRSTMRA LAQAQAQAQA QGTSEGGTPD SPSSTVKSSS
PLPSFARNTV ASSSRSKKDL PSPAVTGTPS KSLARASSQR LPGGRTDSVS SGPLPRSEDK
LGGSIRRVQS VRASNRSSDT PSPQSGREHP LKSSSFSERS TQIRDSISSR TNKPTWK
//
