(data stored in ACNUC5448 zone)

HOGENOM: HS2_PE3288

ID   HS2_PE3288                           STANDARD;      PRT;   2116 AA.
AC   HS2_PE3288; Q6PIF6; Q14786; Q8TEE1;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Myosin-VIIb; (HS2.PE3288).
GN   Name=MYO7B;
OS   HOMO SAPIENS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Primates; Haplorrhini; Simiiformes; Catarrhini;
OC   Hominoidea; Hominidae; Homininae; Homo.
OX   NCBI_TaxID=9606;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HS2.PE3288.
CC       Homo sapiens chromosome 2 GRCh37  sequence 1..243189373 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:MYO7B_HUMAN
CC   -!- FUNCTION: Myosins are actin-based motor molecules with ATPase
CC       activity. Their highly divergent tails are presumed to bind to
CC       membranous compartments, which would be moved relative to actin
CC       filaments. May be have a role in the apical membranes of
CC       transporting epithelia (By similarity).
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6PIF6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6PIF6-2; Sequence=VSP_032930, VSP_032931;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 2 FERM domains.
CC   -!- SIMILARITY: Contains 6 IQ domains.
CC   -!- SIMILARITY: Contains 1 myosin head-like domain.
CC   -!- SIMILARITY: Contains 3 MyTH4 domains.
CC   -!- SIMILARITY: Contains 2 SH3 domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH35615.2; Type=Erroneous initiation;
CC   -!- GENE_FAMILY: HOG000007836 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Homo_sapiens;ENSG00000169994;ENST00000428314;ENSP00000415090.
DR   EMBL; AC010976; - ;
DR   EMBL; AK074183; - ;
DR   EMBL; BC035615; - ;
DR   EMBL; L29147; - ;
DR   UniProtKB/Swiss-Prot; Q6PIF6; Q14786; Q8TEE1; -.
DR   EMBL; AC010976; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; L29147; AAA20910.1; -; mRNA.
DR   EMBL; AK074183; BAB85009.1; -; mRNA.
DR   EMBL; BC035615; AAH35615.2; ALT_INIT; mRNA.
DR   IPI; IPI00889512; -.
DR   IPI; IPI00939150; -.
DR   RefSeq; NP_001073996.1; NM_001080527.1.
DR   UniGene; Hs.154578; -.
DR   UniGene; Hs.677195; -.
DR   ProteinModelPortal; Q6PIF6; -.
DR   SMR; Q6PIF6; 3-811, 966-1581, 1606-2098.
DR   STRING; Q6PIF6; -.
DR   PRIDE; Q6PIF6; -.
DR   Ensembl; ENST00000428314; ENSP00000415090; ENSG00000169994.
DR   GeneID; 4648; -.
DR   KEGG; hsa:4648; -.
DR   UCSC; uc002top.1; human.
DR   CTD; 4648; -.
DR   GeneCards; GC02P120600; -.
DR   H-InvDB; HIX0002437; -.
DR   HGNC; HGNC:7607; MYO7B.
DR   HPA; HPA039131; -.
DR   MIM; 606541; gene.
DR   neXtProt; NX_Q6PIF6; -.
DR   PharmGKB; PA31412; -.
DR   eggNOG; prNOG04352; -.
DR   GeneTree; ENSGT00590000082740; -.
DR   NextBio; 17916; -.
DR   ArrayExpress; Q6PIF6; -.
DR   Bgee; Q6PIF6; -.
DR   CleanEx; HS_MYO7B; -.
DR   Genevestigator; Q6PIF6; -.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003774; F:motor activity; IEA:InterPro.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR000857; MyTH4_dom.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   Gene3D; G3DSA:1.20.80.10; ACBP; 2.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF00612; IQ; 4.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF00784; MyTH4; 2.
DR   Pfam; PF07653; SH3_2; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00295; B41; 2.
DR   SMART; SM00015; IQ; 4.
DR   SMART; SM00242; MYSc; 1.
DR   SMART; SM00139; MyTH4; 2.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF47031; FERM_3-hlx; 2.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS00660; FERM_1; FALSE_NEG.
DR   PROSITE; PS00661; FERM_2; FALSE_NEG.
DR   PROSITE; PS50057; FERM_3; 2.
DR   PROSITE; PS50096; IQ; 4.
DR   PROSITE; PS51016; MYTH4; 2.
DR   PROSITE; PS50002; SH3; 1.
DR   HOGENOMDNA; HS2.PE3288; -.
KW   ENSG000001699941755old_1320000031; ENSP000004150907901old_1320000031;
KW   B9A063_HUMAN; C9JC21_HUMAN; AC010976; AK074183; BC035615; L29147;
KW   Actin-binding; Alternative splicing; ATP-binding; Cell membrane;
KW   Complete proteome; Membrane; Motor protein; Myosin;
KW   Nucleotide-binding; Polymorphism; Reference proteome; Repeat;
KW   SH3 domain.
SQ   SEQUENCE   2116 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSGFRLGDHV WLEPPSTHKT GVAIGGIIKE AKPGKVLVED DEGKEHWIRA EDFGVLSPMH
     PNSVQGVDDM IRLGDLNEAG MVHNLLIRYQ QHKIYTYTGS ILVAVNPFQV LPLYTLEQVQ
     LYYSRHMGEL PPHVFAIANN CYFSMKRNKR DQCCIISGES GAGKTETTKL ILQFLATISG
     QHSWIEQQVL EANPILEAFG NAKTIRNDNS SRFGKYIDIY FNPSGVIEGA RIEQFLLEKS
     RVCRQAPEER NYHIFYCMLM GVSAEDKQLL SLGTPSEYHY LTMGNCTSCE GLNDAKDYAH
     IRSAMKILQF SDSESWDVIK LLAAILHLGN VGFMASVFEN LDASDVMETP AFPTVMKLLE
     VQHQELRDCL IKHTILIRGE FVTRSLNIAQ AADRRDAFVK GIYGHLFLWI VKKINAAIFT
     PPAQDPKNVR RAIGLLDIFG FENFENNSFE QLCINFANEH LQQFFVQHVF TMEQEEYRSE
     NISWDYIHYT DNRPTLDLLA LKPMSIISLL DEESRFPQGT DLTMLQKLNS VHANNKAFLQ
     PKNIHDARFG IAHFAGEVYY QAEGFLEKNR DVLSTDILTL VYSSKNKFLR EIFNLELAET
     KLGHGTIRQA KAGNHLFKSA DSNKRPSTLG SQFKQSLDQL MKILTNCQPY FIRCIKPNEY
     KKPLLFDREL CLRQLRYSGM METVHIRKSG FPIRYTFEEF SQRFGVLLPN AMRMQLQGKL
     RQMTLGITDV WLRTDKDWKA GKTKIFLRDH QDTLLEVQRS QVLDRAALSI QKVLRGYRYR
     KEFLRQRRAA VTLQAWWRGY CNRRNFKLIL VGFERLQAIA RSQPLARQYQ AMRQRTVQLQ
     ALCRGYLVRQ QVQAKRRAVV VIQAHARGMA ARRNFQQRKA NAPLVIPAEG QKSQGALPAK
     KRRSIYDTVT DTEMVEKVFG FLPAMIGGQE GQASPHFEDL ESKTQKLLEV DLDTVPMAEE
     PEEDVDGLAE YTFPKFAVTY FQKSASHTHI RRPLRYPLLY HEDDTDCLAA LVIWNVILRF
     MGDLPEPVLY ARSSQQGSSV MRQIHDTLGR EHGAQVPQHS RSAQVASQLN IGEEALEPDG
     LGADRPMSNL EKVHFIVGYA ILRPSLRDEI YCQICKQLSE NFKTSSLARG WILLSLCLGC
     FPPSERFMKY LLNFIGQGPA TYGPFCAERL RRTYANGVRA EPPTWLELQA VKSKKHIPIQ
     VILATGESLT VPVDSASTSR EMCMHIAHKQ GLSDHLGFSL QVAVYDKFWS LGSGRDHMMD
     AIARCEQMAQ ERGESQRQSP WRIYFRKEFF TPWHDSREDP VSTELIYRQV LRGVWSGEYS
     FEKEEELVEL LARHCYVQLG ASAESKAVQE LLPSCIPHKL YRTKPPDRWA SLVTAACAKA
     PYTQKQVTPL AVREQVVDAA RLQWPLLFSR LFEVITLSGP RLPKTQLILA VNWKGLCFLD
     QQEKMLLELS FPEVMGLATN REAQGGQRLL LSTMHEEYEF VSPSSVAIAE LVALFLEGLK
     ERSIFAMALQ DRKATDDTTL LAFKKGDLLV LTKKQGLLAS ENWTLGQNDR TGKTGLVPMA
     CLYTIPTVTK PSAQLLSLLA MSPEKRKLAA QEGQFTEPRP EEPPKEKLHT LEEFSYEFFR
     APEKDMVSMA VLPLARARGH LWAYSCEPLR QPLLKRVHAN VDLWDIACQI FVAILRYMGD
     YPSRQAWPTL ELTDQIFTLA LQHPALQDEV YCQILKQLTH NSNRHSEERG WQLLWLCTGL
     FPPSKGLLPH AQKFIDTRRG KLLAPDCSRR IQKVLRTGPR KQPPHQVEVE AAEQNVSRIC
     HKIYFPNDTS EMLEVVANTR VRDVCDSIAT RLQLASWEGC SLFIKISDKV ISQKEGDFFF
     DSLREVSDWV KKNKPQKEGA PVTLPYQVYF MRKLWLNISP GKDVNADTIL HYHQELPKYL
     RGFHKCSRED AIHLAGLIYK AQFNNDRSQL ASVPKILREL VPENLTRLMS SEEWKKSILL
     AYDKHKDKTV EEAKVAFLKW ICRWPTFGSA FFEVKQTSEP SYPDVILIAI NRHGVLLIHP
     KTKDLLTTYP FTKISSWSSG STYFHMALGS LGRGSRLLCE TSLGYKMDDL LTSYVQQLLS
     AMNKQRGSKA PALAST
//

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