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ICAM5_RABIT
ID   ICAM5_RABIT             Reviewed;         912 AA.
AC   Q28730;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Intercellular adhesion molecule 5;
DE            Short=ICAM-5;
DE   AltName: Full=Telencephalin;
DE   Flags: Precursor;
GN   Name=ICAM5; Synonyms=TLCN;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Japanese white; TISSUE=Brain;
RX   PubMed=7794412; DOI=10.1016/0896-6273(94)90211-9;
RA   Yoshihara Y., Oka S., Nemoto Y., Watanabe Y., Nagata S., Kagamiyama H.,
RA   Mori K.;
RT   "An ICAM-related neuronal glycoprotein, telencephalin, with brain segment-
RT   specific expression.";
RL   Neuron 12:541-553(1994).
CC   -!- FUNCTION: ICAM proteins are ligands for the leukocyte adhesion protein
CC       LFA-1 (integrin alpha-L/beta-2).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed on neurons in the most rostral segment of
CC       the mammalian brain, the telencephalon.
CC   -!- PTM: Glycosylation at Asn-53 is critical for functional folding.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. ICAM family.
CC       {ECO:0000305}.
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DR   EMBL; L13199; AAA18478.1; -; Unassigned_DNA.
DR   RefSeq; NP_001164621.1; NM_001171150.1.
DR   AlphaFoldDB; Q28730; -.
DR   SMR; Q28730; -.
DR   PRIDE; Q28730; -.
DR   GeneID; 100328960; -.
DR   KEGG; ocu:100328960; -.
DR   CTD; 7087; -.
DR   InParanoid; Q28730; -.
DR   OrthoDB; 731140at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR   GO; GO:0098609; P:cell-cell adhesion; IEA:InterPro.
DR   Gene3D; 2.60.40.10; -; 9.
DR   InterPro; IPR003988; ICAM.
DR   InterPro; IPR013768; ICAM_N.
DR   InterPro; IPR003987; ICAM_VCAM_N.
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; IPR003598; Ig_sub2.
DR   Pfam; PF03921; ICAM_N; 1.
DR   PRINTS; PR01473; ICAM.
DR   PRINTS; PR01472; ICAMVCAM1.
DR   SMART; SM00409; IG; 5.
DR   SMART; SM00408; IGc2; 3.
DR   SUPFAM; SSF48726; SSF48726; 9.
DR   PROSITE; PS50835; IG_LIKE; 3.
PE   2: Evidence at transcript level;
KW   Cell adhesion; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW   Membrane; Phosphoprotein; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..912
FT                   /note="Intercellular adhesion molecule 5"
FT                   /id="PRO_0000014801"
FT   TOPO_DOM        30..826
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        827..847
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        848..912
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          47..127
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          132..232
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          239..324
FT                   /note="Ig-like C2-type 3"
FT   DOMAIN          332..395
FT                   /note="Ig-like C2-type 4"
FT   DOMAIN          403..481
FT                   /note="Ig-like C2-type 5"
FT   DOMAIN          486..561
FT                   /note="Ig-like C2-type 6"
FT   DOMAIN          566..645
FT                   /note="Ig-like C2-type 7"
FT   DOMAIN          659..734
FT                   /note="Ig-like C2-type 8"
FT   DOMAIN          738..819
FT                   /note="Ig-like C2-type 9"
FT   REGION          678..708
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          880..902
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        690..708
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         179
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UMF0"
FT   MOD_RES         181
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UMF0"
FT   CARBOHYD        53
FT                   /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        134
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        192
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        211
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        311
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        366
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        392
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        576
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        639
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        756
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        787
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        788
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        54..97
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        58..101
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        139..195
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        246..297
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        339..378
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        410..465
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        493..546
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        573..638
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        666..717
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        761..806
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   912 AA;  95683 MW;  4DC032853DA0EAE9 CRC64;
     MPGPSPGLRA LLGFWVALGL GILRLSAVAQ EPFWADLQPR VALVERGGSL WLNCSTNCPR
     PERGGLETSL RRNGPEGLRW RARQLVDIRE PETQPVCFFR CAATLQARGL IRTFQRPDRV
     ELVPLPPWQP VGENFTLSCR VPGAGPRGSL TLTLLRGAQE LIRRSFAGEP ARARGAVLTA
     TVLARREDHG ANFSCRAELD LRPQGLALFE NSSAPRQLWT YALPLDSPRL LAPRVLEVDS
     QSLVSCTLDG LFPASEAGVH LALGDKRLNP EVTLEGDAIV ATATATAEEE GIKQLVCAVT
     LGGERRESRE NVTVYSFPAP LLTLSEPSAP EGKLVTVTCT AGARALVTLE GVPAAAPGQP
     AQLQFNASES DDGRSFFCDA TLELDGETLS KNGSAELRVL YAPRLDDADC PRSWTWPEGP
     EQTLRCEARG NPTPAVHCAR SDGGAVLALG LLGPVTRALA GTYRCTAANV QGEAVKDVTL
     TVEYAPALDS VGCPERVTWL EGTEASLSCV AHGVPPPSVS CVRFRQADVI EGLLLVAREH
     AGTYRCEAIN ARALAKNVAV TVEYGPSFEE RSCPSNWTWV EGSEQLFSCE VEGKPQPSVQ
     CVGSEGASEG LLLPLAPLNP SPSDPSVPRD LAPGIYVCNA TNPLGSAVKT VVVSAESPPQ
     MDDSTCPSDQ TWLEGAEAAG PACARGRPSP RVRCSREGAP RPARPRVSRE DAGTYLCVAT
     NAHGSDSRTV TVGVEYRPVV AELAASPSGG VRPGGNFTLT CRAEAWPPAQ ISWRAPPGAP
     NIGLSSNNST LSVPGAMGSH GGEYECEATN AHGHARRITV RVAGPWLWIA VGGAVGGAVL
     LAAGAGLAFY VQSTACKKGE YNVQEAESSG EAVCLNGAGG GAGSGAEGGP EAEDSAESPA
     GGEVFAIQLT SA
 
 
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