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IGSF3_XENLA
ID   IGSF3_XENLA             Reviewed;        1165 AA.
AC   Q5U5A3;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Immunoglobulin superfamily member 3;
DE            Short=IgSF3;
DE   Flags: Precursor;
GN   Name=igsf3;
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 (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
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DR   EMBL; BC084781; AAH84781.1; -; mRNA.
DR   RefSeq; NP_001088456.1; NM_001094987.1.
DR   RefSeq; XP_018103911.1; XM_018248422.1.
DR   AlphaFoldDB; Q5U5A3; -.
DR   GeneID; 495320; -.
DR   KEGG; xla:495320; -.
DR   CTD; 495320; -.
DR   Xenbase; XB-GENE-6253974; igsf3.S.
DR   OMA; AYAVYSQ; -.
DR   OrthoDB; 180654at2759; -.
DR   Proteomes; UP000186698; Chromosome 2S.
DR   Bgee; 495320; Expressed in internal ear and 19 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; -; 8.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR013106; Ig_V-set.
DR   Pfam; PF07686; V-set; 4.
DR   SMART; SM00409; IG; 8.
DR   SMART; SM00406; IGv; 5.
DR   SUPFAM; SSF48726; SSF48726; 8.
DR   PROSITE; PS50835; IG_LIKE; 7.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Immunoglobulin domain; Membrane; Reference proteome;
KW   Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..1165
FT                   /note="Immunoglobulin superfamily member 3"
FT                   /id="PRO_0000320136"
FT   TOPO_DOM        21..1095
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1096..1116
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1117..1165
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          22..139
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          144..262
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          276..386
FT                   /note="Ig-like C2-type 3"
FT   DOMAIN          406..527
FT                   /note="Ig-like C2-type 4"
FT   DOMAIN          545..661
FT                   /note="Ig-like C2-type 5"
FT   DOMAIN          678..800
FT                   /note="Ig-like C2-type 6"
FT   DOMAIN          810..934
FT                   /note="Ig-like C2-type 7"
FT   DOMAIN          951..1067
FT                   /note="Ig-like C2-type 8"
FT   MOTIF           250..252
FT                   /note="EWI motif"
FT   DISULFID        43..121
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        168..246
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        302..376
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        432..511
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        566..645
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        701..779
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        835..918
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        974..1051
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   1165 AA;  129559 MW;  18227222AAC00406 CRC64;
     MGTAAGLLLA ALLLAGTSWA QREVNIQQGP LYRAEGSQIS IWCNVRGYQG PSEQNFLWSI
     YLPSAPEKEI QMVGTSDPSF SYAIYSQRVR SGDIYVERVS GDHALLHIRQ LQEQDAGEYE
     CHTPNTDPTY HGSYSAKMNL HVIPDTLTVS SPAQTLQKVE GGSLQVTCEV SQNSSQHTHL
     SVSWLRISGG EEHEIISLTQ NLSVRAGPTY AQKHSVGDVR MDKLGDSTFR LTLYNLHPSD
     QGEIHCVGTE WIQDPDGTWF PLTQKRSEGT SVTVQPTDKE FNVRLETERR TYGAGDMASL
     RCIIDAQNPA ERLFAVSWAF NSSLIASQSP GGVPSLTGEY AKREDRGEVR VGKDSDIVFS
     LKIFHLRPED SGKYNCRVTE RERGPSGELI DRESKRPKNI PISVLPLRTS LTVTVTANSS
     SVLEGVRLSL TCSVASLAGP QSRISASWHL QDKQGRQREV VRQDRDGVTW AGEQYRERLG
     TGELRLIRSG SDTFSLELEG SQRTDTGSYE CRVAEWVPAT DGEWQLLGER SAQANVDIMA
     LETGFAVTAI TRTPGVSYFD SFDLQCILKP HYPPWVGVSV TWRFQPAGGG DTHDLVTFSR
     AGGVQWGERA GSFRGRSVVE KGDSTHTVKL SVSRASDSEA GKYQCVAELW RWEYRGTWTQ
     LAERASNLLE IRVQRPVPRL QVSKVTRTLS VVEGSQVTLS CSIRSQTGPD SRFAVLWFMR
     QPSGADGKLI VRSNTGMEYG TYAEEASLKG RLQLEVTAPG HYTLTLQGAH ADDSGSYYCQ
     VEEWAMDPNQ AWYRLAEEAS GMTEIRVRVP DANLQLDQIP RNVSALEGQS FTVTCHVLNR
     TLPDSRLSLE WLSWWAGHME RRALVRLTVD GVTILGSVEE ENVAPGLPSR MQVSQPSLGL
     YALTLRGTEV QDTGTYSCLV QEWLQDPRGQ WYKRTEERSG ATYVSVRQPD PALQLDSSLL
     NVSLMEGGHF DLDCVVSSRS RPDSQLAISW SLQGASRGAE QETLLNVDRS GVWAPMAPRW
     EGRLQQLQLS PTLFRLHVPR VGQGDSGNYT CLVQEWLQGP RGNWYLLAQD ESLIGWIRVQ
     SKESNLQSTI CANDALFYLV FFYPFPIFGI LIITILLVRF RHRPTSKPGE GKNGVPLLWI
     KEPHLNYSPT CLEPPVLSIH PGTID
 
 
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