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 27-MAR-2024, entry version 116.
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 GlyCosmos; Q28730; 12 sites, No reported glycans.
DR GeneID; 100328960; -.
DR KEGG; ocu:100328960; -.
DR CTD; 7087; -.
DR InParanoid; Q28730; -.
DR OrthoDB; 4014106at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005178; F:integrin binding; IEA:InterPro.
DR GO; GO:0098609; P:cell-cell adhesion; IEA:InterPro.
DR CDD; cd00096; Ig; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 9.
DR InterPro; IPR003988; ICAM.
DR InterPro; IPR048679; ICAM1_3_5_D2.
DR InterPro; IPR013768; ICAM_N.
DR InterPro; IPR047012; ICAM_VCAM.
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 PANTHER; PTHR13771; INTERCELLULAR ADHESION MOLECULE; 1.
DR PANTHER; PTHR13771:SF9; INTERCELLULAR ADHESION MOLECULE 5; 1.
DR Pfam; PF21146; ICAM1_3_5_D2; 1.
DR Pfam; PF03921; ICAM_N; 1.
DR Pfam; PF13927; Ig_3; 1.
DR PRINTS; PR01473; ICAM.
DR PRINTS; PR01472; ICAMVCAM1.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 3.
DR SUPFAM; SSF48726; Immunoglobulin; 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
//
