ID A0A2U9CLN1_SCOMX Unreviewed; 1686 AA.
AC A0A2U9CLN1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Putative tectonin beta-propeller repeat-containing protein 1 {ECO:0000313|EMBL:AWP17425.1};
GN ORFNames=SMAX5B_020382 {ECO:0000313|EMBL:AWP17425.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP17425.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP17425.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TECPR1 family.
CC {ECO:0000256|ARBA:ARBA00005966}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP026260; AWP17425.1; -; Genomic_DNA.
DR Proteomes; UP000246464; Chromosome 18.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0007009; P:plasma membrane organization; IEA:InterPro.
DR CDD; cd13300; PH1_TECPR1; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR006624; Beta-propeller_rpt_TECPR.
DR InterPro; IPR013606; I-BAR_dom.
DR InterPro; IPR010482; Peroxin.
DR InterPro; IPR006614; Peroxin/Ferlin.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR23250; DYSFERLIN-RELATED; 1.
DR PANTHER; PTHR23250:SF11; TECTONIN BETA-PROPELLER REPEAT-CONTAINING PROTEIN 1 ISOFORM X1; 1.
DR Pfam; PF06462; Hyd_WA; 4.
DR Pfam; PF08397; IMD; 1.
DR Pfam; PF06398; Pex24p; 2.
DR Pfam; PF07653; SH3_2; 1.
DR Pfam; PF19193; Tectonin; 1.
DR SMART; SM00694; DysFC; 2.
DR SMART; SM00693; DysFN; 2.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00706; TECPR; 11.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51338; IMD; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 1..248
FT /note="IMD"
FT /evidence="ECO:0000259|PROSITE:PS51338"
FT DOMAIN 323..386
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 286..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1654..1686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..433
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1686 AA; 188114 MW; 8133966FEE233C93 CRC64;
MSRAPDGVSK LTESTFKNVM EQFNPGLRNL VNLGKSYEKS VTAMTLSGKV YFEAVSKIGE
NAMVSPVSRE LGVVLMEMAE VHRKVHIELE ENFKSFHKEI IIELEKKTEM DVKYMNATFK
RYQSEHKLKQ DSLERSQTDL KKIRRKSQGK HSSKYEIKEN EYMETISSRQ TDMQKFIADG
CREALLEEKR RFCFLADKHC MFSYQIGNFY EKAKEMLAMK LPSWQDKCTD ITKVPDTVAT
MIEGLSTPEQ SPQVEHCNRN NAASLMPPPA PPLKAQISPL AIMFNPEPRS PLTSASDHNS
DQGSLGEGSL SRSASQSSGL NVARRHRVRT IFPHTSGNNN TLLSFDEGDI ISLLIHEEKD
GWLYGELDRT RQRGWFPSSY CRAYSEPAIT YSNLGTPVRR LSVASLPEQE EEEPVLIPPP
DYGDDPSSPA VPSTPSPQNT VSLVNGTAKA SFLGVLKMSI GSHTDYDLTA GAAMPVSLLW
AVDVYGRVYS LSTAGQQWEH CHDAQLEFKR VTAAEQCCWG IACDNNIYLN VHASDLPVRY
QEETYENQRW NPVDSFSERL LPSDRWQWSD VTGLQHQPLD SFRLPSNSWE WEGDWYMDEN
FEGEPTDKEG WTYAIDFPAN YTKDKKWNSC VRRRRWLRYR RYKAMDTWAK IPSQQTTLPD
PFSDISCGGW EISEEPRGRL SLWAVSLQGK VWFREGIDHH SPEGSLWEEV PLPGEVVQLS
CGPGDVVWAV LWEGQLIVRE GIGRDSPKGT SWAVVESPSL DVGAIHVAVG ISVVWVVTKD
NKVWFRRGVN SHNPCGSGWI SMVGEMIMLN IGLNDQVWGI GCEDRAVYFR QGVTSSELSG
KTWKVINVPR DGDRSHSSAS ANSLQSAGCY FCGEVGGQSV VSDVESDPEK ASTDGATGLV
MSDSKCEAFA APADHTSDQP PDTLKPRIPK VTSDSFISEL VSDREPAKTS RELGSAAPAL
LEEETLPDEG EVNAPCSATL STSQSGVPLD PQWSNVDLEE TQVQLAQTGV ALESADTCSL
SSVATYTLAM DDPYGADEPP LWAWVSGGGC SVDSHSQLNW FNCSINTSAL VQSVQSMSLS
VTPAQTAAWR RQIFDQFSER TKREMDSFRH YEQAIEQSVW VKKGTMQWWR DWKPHKWIDV
QFALEQFSGP EGNKDGIFFI YYNFYEEKKY LHAFINEITI LVPVLNDSKH TFAIYTPERT
KQRWPIRLAA ATELEMRDWL ALLSVSCCDS RGLQGPPSKQ AIWSITCKGD IFVSEPSPAL
EAMPYPTPCD QMFWRQVGGH LRVVECNSVG IVWGIGYDHT AWVYTGGYGG GFFQGLASST
DNIHTQTDIK SVYIYENQRW NPVSGYTNRG LPTDRYMWSD ASGLHECTKT NTKPPSPQWT
WVSDWVIDYS VSGGTDREGW QFAADFPASY HGYKTMKDFV RRRRWGRKCK LTTTGPWQEI
PPIPLSDVTI LPHAAQSSVD VVPLWAISNK GDVLCRLGVT ALTPAGSSWL HVGTDQPFKS
ITIGATSQVW GIAKDGSAFY RGSVSPQSPA GDCWYHIPSP AKQKLKHVSV GRTSVYTVDE
NGNLWYRQDV TPSYPQGSSW EHISNNVRKV SVGPLDQVWI IADKVQGSHS LSCGTVCHRL
GVQPMEPKGQ SWDYGIGGGW DHVTVRGNSL EPPRIHLPSL TGPSSPAPRS LLPVRSGEAN
GNAAGC
//