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TIP_RAT
ID   TIP_RAT                 Reviewed;         610 AA.
AC   Q8R4E1;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=T-cell immunomodulatory protein;
DE            Short=Protein TIP;
DE   AltName: Full=CDA08-like protein;
DE   AltName: Full=Integrin-alpha FG-GAP repeat-containing protein 1;
DE   AltName: Full=Linkin {ECO:0000250|UniProtKB:Q8TB96};
DE   Flags: Precursor;
GN   Name=Itfg1 {ECO:0000312|RGD:619898};
GN   Synonyms=Cda08 {ECO:0000312|RGD:619898},
GN   Lnkn-1 {ECO:0000250|UniProtKB:Q8TB96}, Tip {ECO:0000250|UniProtKB:Q8TB96};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Cerebellum;
RA   Vie-Luton M.-P., Francon J.;
RL   Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-480, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=24090084; DOI=10.1021/pr400783j;
RA   Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA   Graham M.E., Packer N.H., Cordwell S.J.;
RT   "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT   heterogeneity.";
RL   J. Proteome Res. 12:5791-5800(2013).
CC   -!- FUNCTION: Modulator of T-cell function. Has a protective effect in
CC       graft versus host disease model (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with RUVBL1, RUVBL2 and alpha-tubulin.
CC       {ECO:0000250|UniProtKB:Q8TB96}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Cell membrane
CC       {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the TIP family. {ECO:0000305}.
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DR   EMBL; AF480856; AAL84891.1; -; mRNA.
DR   AlphaFoldDB; Q8R4E1; -.
DR   STRING; 10116.ENSRNOP00000021711; -.
DR   GlyGen; Q8R4E1; 11 sites, 2 N-linked glycans (1 site).
DR   iPTMnet; Q8R4E1; -.
DR   PhosphoSitePlus; Q8R4E1; -.
DR   jPOST; Q8R4E1; -.
DR   PaxDb; Q8R4E1; -.
DR   PRIDE; Q8R4E1; -.
DR   RGD; 619898; Itfg1.
DR   eggNOG; KOG4550; Eukaryota.
DR   InParanoid; Q8R4E1; -.
DR   PhylomeDB; Q8R4E1; -.
DR   PRO; PR:Q8R4E1; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   Gene3D; 2.130.10.130; -; 1.
DR   InterPro; IPR013517; FG-GAP.
DR   InterPro; IPR028994; Integrin_alpha_N.
DR   InterPro; IPR024881; Tip.
DR   PANTHER; PTHR13412; PTHR13412; 1.
DR   Pfam; PF13517; FG-GAP_3; 1.
DR   SUPFAM; SSF69318; SSF69318; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Glycoprotein; Membrane; Reference proteome; Repeat;
KW   Secreted; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..610
FT                   /note="T-cell immunomodulatory protein"
FT                   /id="PRO_0000034356"
FT   TRANSMEM        564..584
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REPEAT          98..135
FT                   /note="FG-GAP 1; atypical"
FT   REPEAT          153..183
FT                   /note="FG-GAP 2; atypical"
FT   REPEAT          256..291
FT                   /note="FG-GAP 3; atypical"
FT   CARBOHYD        35
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        94
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        123
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        138
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        145
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        150
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        175
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        241
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        351
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        369
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        480
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0007744|PubMed:24090084"
SQ   SEQUENCE   610 AA;  67337 MW;  F5943D993D7D1CBA CRC64;
     MAAGLLPSAR AVLALLFLGL ALLSVGPAPA QALHNVTAEL FGGEAWGTLA AFGDLNSDKQ
     TDLFVLRERN DLIVFLADQS APYFKPKVKV SLKNFSALVT SVVPGDYDGD SQMDVLLTYF
     PQNHSNNELG AVIFWGQNQT LDPKNMTILN RTFHDQPLIM DFNGDLIPDV FAITNESSQP
     QILLGGDLSW HPALTTKSKM RDPHSRAFID LTEDFTADLF LTTLSASNTF QFEIWENLGG
     NFSIRSVFEK PKNLVVVGQS AFADFDGDGH MDHLLPGCED KDCQKSAIYL MRSGTGQWAP
     VLQDSSNKGT LWGFVPFVHE ERPTAIPVPL TLHIGDYNMD GYPDALAILK NTSGSNQQAF
     LLENVPCNNA SCEEVHRMFK VYWDLAGLNL IKDAMVATFF DIYEDGTLDI IVLSKGYTKS
     DVAIHTLKNN FEADAYFVKV IVLSGLCSSD CPRKITPFGV NQPGPYIMYT TVDANGYLKN
     GSAGQLSQSA HLALQLPYNV LGLGRSANFL DHLFVGIPRP SGEKSIRKQE WTAIIPNSQL
     MVIPYPHSVP RSWSAKLYLT PSNIVLLTAV ALTGVCVFIL AIIAILHWQE KKADDREKRQ
     EAHRFHFDAM
 
 
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