T161A_XENLA
ID T161A_XENLA Reviewed; 489 AA.
AC Q6GMB1;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Transmembrane protein 161A;
DE Flags: Precursor;
GN Name=tmem161a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May play a role in protection against oxidative stress.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TMEM161 family. {ECO:0000305}.
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DR EMBL; BC074159; AAH74159.1; -; mRNA.
DR RefSeq; NP_001086075.1; NM_001092606.1.
DR AlphaFoldDB; Q6GMB1; -.
DR DNASU; 444504; -.
DR GeneID; 444504; -.
DR KEGG; xla:444504; -.
DR CTD; 444504; -.
DR Xenbase; XB-GENE-6254899; tmem161a.L.
DR OrthoDB; 734854at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 444504; Expressed in neurula embryo and 19 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR019395; Transmembrane_161A/B.
DR PANTHER; PTHR13624; PTHR13624; 1.
DR Pfam; PF10268; Tmemb_161AB; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..489
FT /note="Transmembrane protein 161A"
FT /id="PRO_0000288087"
FT TOPO_DOM 24..98
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..134
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..166
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..224
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..264
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..304
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 326..370
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 392..459
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..480
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 481..489
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 413..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 489 AA; 56194 MW; CC6989FDAC24C491 CRC64;
MAVMGIQMVV TLLVASLMQR VSPHYSFGRW LLCNGSLFRY KHPTEEELRT LAGKQKPKAK
KERRTNGVAE EKPLTVPKDI DLRLDTQPIN TMDALVLRYF LEYQWFIDFA LYSTIIYLFT
EAYYCVVDAQ NEINIGVLWC LMSIIFSIKV LFTVMKHYFR SEEGGERSVC MTFAFFFLLI
AMIVTIVRDE YLEFGLEPGL ASVCHNLENF LAQQGWQWSM PFVKLAFKIA LVALCAFLGG
CLTFPGLRLA QTHLDALKMA ADRPMLQLLL HMSFLPPVIV VVLWIRPITR DFLLNAPMGK
ESVELMSNSA YNTFRLWIIV LLCLLRFCLT RFHLQAYLCL ADRWVEQMKR EAGRISMLEI
QRKISRIFCY LTVVALQYLA PVILTFHCVF MLKSLGDYSW GLYPEPPGFS PVVDSSPVQS
HSPTSEEEED TEDVQAAVEQ IMGVLTSLRG LFTPLFFRGI FSFLTWWVSV CQIITSLFGL
YFHQYLGAS