F1712_XENLA
ID F1712_XENLA Reviewed; 821 AA.
AC A1L3I3;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Protein FAM171A2;
DE Flags: Precursor;
GN Name=fam171a2;
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=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the FAM171 family. {ECO:0000305}.
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DR EMBL; BC130114; AAI30115.1; -; mRNA.
DR RefSeq; NP_001091228.1; NM_001097759.1.
DR AlphaFoldDB; A1L3I3; -.
DR DNASU; 100037014; -.
DR GeneID; 100037014; -.
DR KEGG; xla:100037014; -.
DR CTD; 100037014; -.
DR OMA; WVIVTAS; -.
DR OrthoDB; 615320at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 100037014; Expressed in brain and 19 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR018890; FAM171.
DR PANTHER; PTHR31626; PTHR31626; 1.
DR Pfam; PF10577; UPF0560; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..821
FT /note="Protein FAM171A2"
FT /id="PRO_0000328773"
FT TOPO_DOM 32..317
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 339..821
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 411..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..489
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..611
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..752
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..788
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..821
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 821 AA; 89153 MW; 6C9A046AE2C2868D CRC64;
MGRARDSGKR SGGPPCSFLL LLLLSCGGGR GKSLLGAAGA QDFHIKVQVY ENGDLSPLAS
AAVEIFGNQS SLASGVTDQD GVAVLGISYR LGTWVLVSAT KRGFVTNSVP WRVDRLPLYA
SVSLYLVPER PATLILYEDI VQILLGSPGA RSQPWVQFQR KAARLPRSST YNQLTSSLTT
ASTRHQMRGF PAFIGTEPES ANGGNTSWVE LLPVAAISVH LFSGNGSEVH LSGPVQLSLP
LPPESGLTTS SSVPAWRYEP KVGVWIRSGM GLVRRDGQQL YWSFVSPKLG YWAAAIPSSG
RGMLSLMSGV DIAGYHTIFL LSILGALTLL VLILLCLLIY YCRRRCLKPR QQHHKLQLSG
LSEPKRDQAT STSRLNLIST SHLDSTSTAD SDLRTPVLRS AFSSREDFCK SGGRSSFQHS
ADTLPLRPGS RDEYPLKSAR SGDLLESEDS KRGYGTGGKG QQRRRGGRGG VRDPPPSPPP
LPPPFKHVIG DSKPPDYLMT QSADPLSRPT SLTQPGQFIF CGSIDHMKEG SYRHAMPTLV
IPAHYMRLSS EENQGGQGEE QSESESGSTQ VSHAHHFAPQ DHAQRQQLLQ QGHGYQQGAT
ASSQDQEGKG WGNHGSVTIP VVFNESTMAQ LNGELQALTE KKLLELGVKP HPRAWFVSLD
GRSNAQVRHS YIDLQAGDKT RSNDASLDSG VDVNEIKVKL GPEERSGKAQ LQPSNLTYSK
LVFAEEGEQS LSESRTGGGC SPEDSSLTPL LDEGSETCLP MSRRGRSRGD SSRSSTSELR
RDSMTSPDED LNDQSEGGDD QDKKSPWQKR EERPLMVFNV K