TMC3_CHICK
ID TMC3_CHICK Reviewed; 1138 AA.
AC Q5YCC7;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Transmembrane channel-like protein 3;
GN Name=Tmc3 {ECO:0000312|EMBL:AAT85601.1};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAT85601.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=15857715; DOI=10.1016/j.neuroscience.2005.01.046;
RA Mutai H., Mann S., Heller S.;
RT "Identification of chicken transmembrane channel-like (TMC) genes:
RT expression analysis in the cochlea.";
RL Neuroscience 132:1115-1122(2005).
CC -!- FUNCTION: Probable ion channel. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in a range of tissues including cerebrum,
CC cerebellum, retina, cochlea, lung, liver and heart. Also expressed in
CC the apical, medial and basal portions of the basillar papilla.
CC {ECO:0000269|PubMed:15857715}.
CC -!- SIMILARITY: Belongs to the TMC family. {ECO:0000255}.
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DR EMBL; AY581310; AAT85601.1; -; mRNA.
DR RefSeq; NP_001005820.1; NM_001005820.1.
DR AlphaFoldDB; Q5YCC7; -.
DR STRING; 9031.ENSGALP00000010288; -.
DR PaxDb; Q5YCC7; -.
DR PRIDE; Q5YCC7; -.
DR GeneID; 415470; -.
DR KEGG; gga:415470; -.
DR CTD; 342125; -.
DR VEuPathDB; HostDB:geneid_415470; -.
DR eggNOG; ENOG502QQGX; Eukaryota.
DR InParanoid; Q5YCC7; -.
DR PhylomeDB; Q5YCC7; -.
DR PRO; PR:Q5YCC7; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0008381; F:mechanosensitive ion channel activity; IBA:GO_Central.
DR InterPro; IPR038900; TMC.
DR InterPro; IPR012496; TMC_dom.
DR PANTHER; PTHR23302; PTHR23302; 1.
DR Pfam; PF07810; TMC; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Ion channel; Ion transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1138
FT /note="Transmembrane channel-like protein 3"
FT /id="PRO_0000259604"
FT TOPO_DOM 1..155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..202
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..233
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..327
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 349..369
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 391..401
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 423..508
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 509..529
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 530..569
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 570..590
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 591..618
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 619..639
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 640..676
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 677..697
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 698..1138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 29..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 973..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1065..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..859
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..1002
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1074..1095
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1138 AA; 128763 MW; 192B053DFFE274C9 CRC64;
MEAAPGTAAA AAKPAKSCKK YRMGKRHANI YTYQEPPHSN SDEDISEEKA DSQDPEQVFQ
NIQYQKEVMS NIRCRPWPMR QKLRVLRQAK EIVLKYEGRL TRTRGYQAAG AELWRKFLRL
AYNFVVLFIP WEMRIKKIES HFGSGVASYF IFLRWLFGIN IVLTIMTGAF VVLPELLAGA
PFGSTVSKTI RQEDLKTAQD LDTIWSLGGY LQYSVLFYGY YGSDRKIGKA GYRLPLAYFL
VGMAVFAYSF IILLKKMAKN SRMSLASASD ENYTFCWRLF CAWDYLIGNP EAAESKAAAI
VNSIREAILE EQEKKKSKNL AVTISLRIIA NILVLLSLTG SIYIIYFVVD RSQKLENNKR
ELTLWEKNEV SVVVSLITMI APSAFELVAA LEMYHPRTTL RFQLARVLVL YLGNLYSLII
ALLDKVNSMS VTNSIYSIYQ VSNNSTPSSA TGTPAKEDTL SATISDAQMN SSESHAQSLP
TAGSLVNNTA SSNSAQNQCW ETYVGQEMLK LSIIDMIFTV ASILLIDFFR GLCVRYLSDC
WCWDLESKFP EYGEFKIAEN VLHLVYNQGM IWMGAFFSPC LPAFNVLKLI GLMYLRSWAV
LTCNVPHQQV FRASRSNNFY LAMLLFMLFL CMLPTIFAIA RYKPSLSCGP FSGQEKIYDI
VSETIQNDFP AWFNSVIAYI SSPVVVLPAL LLLFMLIYYL QSIARSLKFT NNQLRMKIQA
ERTEDKKKVV QMAVGQNLVD IPDDQIMSDF TQNSEGTRFQ SLDGSDKRPD KDGGLISQES
SVRASTPRKN GSVLNFESPV SKGTRIQTIS QTVPHAVPST DVARPVNTTP TTSASLTPAP
SVSSAQKPRN DHTTNRYPSV VHGSASELCK TKPYTPVTFK KRIGDVHSEP LFRKSIRQVN
PDAFGAGAPV FVGRRPHATR YFIVNENEPR KKSARSTSRL QRQFRIEEPE DIVELYPCNV
RRYVVQTPQC MYSPHPSEDE EDEEALGRHY VKRSHRPRSL SDLRPAPRFY IGDRADGHVL
TSKVHYKSWD DGFELDLDRP PYAYKKVHLK NVEADQHYLE PQVKPKTKHM LEQSLTESDS
VSIESSSDPQ NSSNDQYIQV IHSKEKYLKP GTKLTKKKSN TNIELNMSEP NELVCSNV
