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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
 
 
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