TIP_MOUSE
ID TIP_MOUSE Reviewed; 610 AA.
AC Q99KW9; E9QQ11; Q9D6X1;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=T-cell immunomodulatory protein;
DE Short=Protein TIP;
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|MGI:MGI:106419};
GN Synonyms=D8Wsu49e {ECO:0000312|MGI:MGI:106419},
GN Lnkn-1 {ECO:0000250|UniProtKB:Q8TB96}, Tip {ECO:0000250|UniProtKB:Q8TB96};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12598909; DOI=10.1038/nbt797;
RA Fiscella M., Perry J.W., Teng B., Bloom M., Zhang C., Leung K., Pukac L.,
RA Florence K., Concepcion A., Liu B., Meng Y., Chen C., Elgin E.C.,
RA Kanakaraj P., Kaufmann T.E., Porter J., Cibotti R., Mei Y., Zhou J.,
RA Chen G., Roschke V., Komatsoulis G., Mansfield B., Ruben S., Sanyal I.,
RA Migone T.-S.;
RT "TIP, a T-cell factor identified using high-throughput screening increases
RT survival in a graft-versus-host disease model.";
RL Nat. Biotechnol. 21:302-307(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Pancreas, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Modulator of T-cell function. Has a protective effect in
CC graft versus host disease model. {ECO:0000269|PubMed:12598909}.
CC -!- SUBUNIT: Interacts with RUVBL1, RUVBL2 and alpha-tubulin.
CC {ECO:0000250|UniProtKB:Q8TB96}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Membrane {ECO:0000305};
CC Single-pass type I membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TIP family. {ECO:0000305}.
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DR EMBL; AK009867; BAB26552.1; -; mRNA.
DR EMBL; AC117185; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC158357; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003977; AAH03977.1; -; mRNA.
DR CCDS; CCDS40424.1; -.
DR RefSeq; NP_082283.2; NM_028007.3.
DR AlphaFoldDB; Q99KW9; -.
DR IntAct; Q99KW9; 1.
DR MINT; Q99KW9; -.
DR STRING; 10090.ENSMUSP00000034140; -.
DR GlyConnect; 2753; 4 N-Linked glycans (2 sites).
DR GlyGen; Q99KW9; 10 sites, 4 N-linked glycans (2 sites).
DR PhosphoSitePlus; Q99KW9; -.
DR EPD; Q99KW9; -.
DR jPOST; Q99KW9; -.
DR MaxQB; Q99KW9; -.
DR PaxDb; Q99KW9; -.
DR PeptideAtlas; Q99KW9; -.
DR PRIDE; Q99KW9; -.
DR ProteomicsDB; 259455; -.
DR Antibodypedia; 14372; 171 antibodies from 23 providers.
DR DNASU; 71927; -.
DR Ensembl; ENSMUST00000034140; ENSMUSP00000034140; ENSMUSG00000031703.
DR GeneID; 71927; -.
DR KEGG; mmu:71927; -.
DR UCSC; uc009mqf.2; mouse.
DR CTD; 81533; -.
DR MGI; MGI:106419; Itfg1.
DR VEuPathDB; HostDB:ENSMUSG00000031703; -.
DR eggNOG; KOG4550; Eukaryota.
DR GeneTree; ENSGT00390000013367; -.
DR HOGENOM; CLU_020272_2_0_1; -.
DR InParanoid; Q99KW9; -.
DR OMA; PGDWIPW; -.
DR OrthoDB; 790976at2759; -.
DR PhylomeDB; Q99KW9; -.
DR TreeFam; TF105620; -.
DR BioGRID-ORCS; 71927; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Itfg1; mouse.
DR PRO; PR:Q99KW9; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q99KW9; protein.
DR Bgee; ENSMUSG00000031703; Expressed in ventral tegmental area and 257 other tissues.
DR Genevisible; Q99KW9; MM.
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 Glycoprotein; Membrane; Reference proteome; Repeat; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..610
FT /note="T-cell immunomodulatory protein"
FT /id="PRO_0000034355"
FT TRANSMEM 565..585
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 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:0000255"
FT CONFLICT 269
FT /note="G -> V (in Ref. 1; BAB26552)"
FT /evidence="ECO:0000305"
FT CONFLICT 521
FT /note="S -> P (in Ref. 3; AAH03977)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 610 AA; 67465 MW; 123667168AB22BE9 CRC64;
MAAGRLPSAR AVLAPLFLGL ALLSVGPAPA RALHNVTAEL FGAEAWGTLA AFGDLNSDKQ
TDLFVLRERN DLIVFLADQS APYFKPKVKV SLKTLSALVT SVVPGDYDGD SQMDVLLTYF
PQNHTNSELG AVIFWGQNQT LDPKNMTILN RTFHDQPLIM DFNGDLIPDV FGITNESSQP
QILLGGDLSW HPALTTKSKM RDPHSHAFID LTEDFTADLF LTTLTASNAF QFEIWENLGG
NFSIHSVFEK PKNLVVVGQS AFADFDGDGH MDHLLPGCED KDCQKSAIYL MRSGTGQWVP
VLQDFSNKGT LWGFVPFVHE EQPTTIPIPL TLHIGDYNMD GYPDALAILK NTSGSNQQAF
LLENVPCNNA SCEEVHRMFK VYWDLAGLNL IKDAIVATFF DIYEDGILDI IVLSKGYTKN
DVAIHTLKNN FEADAYFVKV IVLSGLCSND CPRKITPFGV NQPGPYIMYT TVDANGYLKN
GSAGQLSQSA HLALQLPYNV LGLGRSANFL DHLFVGIPRP SGEKSIRKQE WTAIIPNSQL
IVIPYPHNVP RSWSAKLYLT PSNIVLLTAV ALIGVCIFIL AIIAILHWQE KKADDREKRQ
EAHRFHFDAM
