ID A0A091WBB4_OPIHO Unreviewed; 1829 AA.
AC A0A091WBB4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Melanoma inhibitory activity protein 3 {ECO:0000313|EMBL:KFR12947.1};
DE Flags: Fragment;
GN ORFNames=N306_05772 {ECO:0000313|EMBL:KFR12947.1};
OS Opisthocomus hoazin (Hoatzin) (Phasianus hoazin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Opisthocomiformes; Opisthocomidae;
OC Opisthocomus.
OX NCBI_TaxID=30419 {ECO:0000313|EMBL:KFR12947.1, ECO:0000313|Proteomes:UP000053605};
RN [1] {ECO:0000313|EMBL:KFR12947.1, ECO:0000313|Proteomes:UP000053605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N306 {ECO:0000313|EMBL:KFR12947.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004389}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
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DR EMBL; KK735175; KFR12947.1; -; Genomic_DNA.
DR STRING; 30419.A0A091WBB4; -.
DR PhylomeDB; A0A091WBB4; -.
DR Proteomes; UP000053605; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR23158; MELANOMA INHIBITORY ACTIVITY-RELATED; 1.
DR PANTHER; PTHR23158:SF54; TRANSPORT AND GOLGI ORGANIZATION PROTEIN 1 HOMOLOG; 1.
DR Pfam; PF07653; SH3_2; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Reference proteome {ECO:0000313|Proteomes:UP000053605};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 1..62
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 102..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1043..1115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1404..1431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1628..1829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1197..1364
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1466..1620
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 115..129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..324
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..588
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..646
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..708
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..782
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..815
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..865
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1066..1097
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1722..1737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1746..1829
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFR12947.1"
FT NON_TER 1829
FT /evidence="ECO:0000313|EMBL:KFR12947.1"
SQ SEQUENCE 1829 AA; 204262 MW; 2A95C3AD73129EFF CRC64;
LMCRGKAMQD FKGPDCRFVN FKKGEAVYVY YKLIGKSTEL WAGSVGSDFG YFPKDLLEIN
HNYSNEELEL PTDETDFVCF DGGRDDFDNY NVDELLKQEM IANEGETESS DPGAKPAEGT
ERDEEIEQAD TINSPDALET ANLELSTEED NEALAMTEEL DSSLTGGTEN TGGDSSVNSH
EEDSQGDHVA HEHLKGMLHG KLKGLESENT KNTSIPQGET SQLDKESEEV NAYTLLNREF
SVNLKTKFGS TADAVVSDDE VTGLVTSLED DFNEDLSINT YDAEEEPDFA DQSEEIPLLS
FTAEEEITSP ADLDDDENDD IESQNHELED AKGATELNNQ RDNEEEHDSD ALILKDAFSR
SKKLGDSVHE DRFESQQIKE KEDEVMIISK REAPATTQPG DLSKELLRKE PVGRGALGSG
EKANETEQFE EQLTVDGTES YTEELKSTAV PDPHVLPNPG DDLESKLLFK TKQDALKPPD
GDINNSPERT LLTQIEKDEK KFEDDTLEEV LESDLKHKNL WEKTKEKGRA EDKHSVDVPA
KLVEEVKNAS QSDLGDTDLL KEKLEHGMPA VEKEPLSHEE DLKQTGETDR ENQTTASLNK
ESGIKRGSMK ETPAGEGDPS HGGDVKQPRP WENEAEYSEA DTKEALSRNL GRMTVFEESI
EKSLPEEKST SITQNTNTEH LTRQGTAQLQ SEEPDAEDDP DLKQAEEELL EDENAASAKL
SQAKAANAQG DMLNATSADP ELEVRSQAVL GTATPTYEIG EETNSFSKEV KKTISMQDAT
ESGNKEVDIP VGEDARLDEM ERFMEDDEES SEAEEPSAVE EHNFQSPDVE DNNDFNQRKD
HLPEDISQKD SKEVQNSEHT GDDHQQPAHF PSPADSSAAT NDTVTDFSES VKRLTIIRNF
LDEKRVMRLR KYLGLQHMVR IEAIFHDMKV EMELAQKASH NNEDIEKALD QILEFSESSI
MDIVGKVLDS RVAENKEEVV REMDLYDDES ALIDDLQELI YSLRSKYSSA SESVPLAFIP
EQEDDQLHVQ GRIVSISNAN AIDKSNQKFQ QPEDKTPEQP IEEEEEEEKR AANVPPEHEE
ANFADNREAE EGYNSERGSL LEDTSFGPVD SGQSAREDTV AGNLLDLVFN ENTFRIVNVV
GFQLVATLPE EIRPGPDFHG LPWEPVIITA LVGIATLAII FWRTCLSVKS RMYQVTEKQL
AEKIKNLLQE KTEILEKMSE YNQKIKEAKE SVKVAQEEKD ILCDETAGLK DTVKGLEEAN
RQLDDKVKNL HTMLETERKK NEKKQNKISE TQKSLEKLQE AISVHSVELS EVQIALNEAK
LSEEKVKSEL HHVQEENVRL KTSKEQLLKE AEGWSERHTE LSEQIKLYQK SQKDIEEALA
YKENEIEVLT NCIMQLKQLD MDSASEAKKD GEGGEWSAGD DLANGELPDN ESEKMKTQIK
QMMDVSRVKT MLSIVEEDRN LLQSKLSDEV TARHELEEQI KKLEHDSCSL QSDKARLENE
CKTLQQKVEI LGELYQQKEM ALQKKLTQEE YERQEKEQKL SAADEKALLA IEEVKVYKQR
IQDMEEELQK TERSYKNQIA AHEKKAHDNW LIARSAERAL AEEKREAANL RQKLIEVNQK
IVMLQRPLIV KPTPGRPDRQ VPPRRGPLSR DGSFGPSPVS GGNPSPTQMI EVPARPLSAP
RREGSRGEFV VDGPPVPRRP PELPGRMSVP DLGPAVASLI SSGPGPRTSS PSTAVDGVAN
ASPKGPPSFP GTPIMTAPVM GPPPPPPVRY GPPPAPLRGH FGPRPLPVPL VRGAPLPPPA
ARDFLPGPPL GMRDLPPGPL PPPPDPRGY
//
