ID   SEM4A_BOVIN             Reviewed;         762 AA.
AC   Q5EA85;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Semaphorin-4A;
DE   Flags: Precursor;
GN   Name=SEMA4A;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
CC   -!- FUNCTION: Cell surface receptor for PLXNB1, PLXNB2, PLXNB3 and PLXND1
CC       that plays an important role in cell-cell signaling (By similarity).
CC       Regulates glutamatergic and GABAergic synapse development (By
CC       similarity). Promotes the development of inhibitory synapses in a
CC       PLXNB1-dependent manner and promotes the development of excitatory
CC       synapses in a PLXNB2-dependent manner (By similarity). Plays a role in
CC       priming antigen-specific T-cells, promotes differentiation of Th1 T-
CC       helper cells, and thereby contributes to adaptive immunity (By
CC       similarity). Promotes phosphorylation of TIMD2 (By similarity).
CC       Inhibits angiogenesis (By similarity). Promotes axon growth cone
CC       collapse (By similarity). Inhibits axonal extension by providing local
CC       signals to specify territories inaccessible for growing axons (By
CC       similarity). {ECO:0000250|UniProtKB:Q62178}.
CC   -!- SUBUNIT: Interacts with PLXNB1, PLXNB2, PLXNB3, PLXND1 and TIMD2 (By
CC       similarity). {ECO:0000250|UniProtKB:Q62178}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q62178};
CC       Single-pass type I membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
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DR   EMBL; BT020684; AAX08701.1; -; mRNA.
DR   RefSeq; NP_001068908.1; NM_001075440.1.
DR   AlphaFoldDB; Q5EA85; -.
DR   SMR; Q5EA85; -.
DR   STRING; 9913.ENSBTAP00000016223; -.
DR   PaxDb; Q5EA85; -.
DR   PRIDE; Q5EA85; -.
DR   GeneID; 510239; -.
DR   KEGG; bta:510239; -.
DR   CTD; 64218; -.
DR   eggNOG; KOG3611; Eukaryota.
DR   InParanoid; Q5EA85; -.
DR   OrthoDB; 64683at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0045499; F:chemorepellent activity; IBA:GO_Central.
DR   GO; GO:0030215; F:semaphorin receptor binding; IBA:GO_Central.
DR   GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR   GO; GO:0050919; P:negative chemotaxis; IBA:GO_Central.
DR   GO; GO:0048843; P:negative regulation of axon extension involved in axon guidance; IBA:GO_Central.
DR   GO; GO:0001755; P:neural crest cell migration; IBA:GO_Central.
DR   GO; GO:0030335; P:positive regulation of cell migration; IBA:GO_Central.
DR   GO; GO:1904891; P:positive regulation of excitatory synapse assembly; ISS:UniProtKB.
DR   GO; GO:1905704; P:positive regulation of inhibitory synapse assembly; ISS:UniProtKB.
DR   GO; GO:0071526; P:semaphorin-plexin signaling pathway; IBA:GO_Central.
DR   Gene3D; 2.130.10.10; -; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR002165; Plexin_repeat.
DR   InterPro; IPR016201; PSI.
DR   InterPro; IPR001627; Semap_dom.
DR   InterPro; IPR036352; Semap_dom_sf.
DR   InterPro; IPR027231; Semaphorin.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR11036; PTHR11036; 1.
DR   Pfam; PF01437; PSI; 1.
DR   Pfam; PF01403; Sema; 1.
DR   SMART; SM00423; PSI; 1.
DR   SMART; SM00630; Sema; 1.
DR   SUPFAM; SSF101912; SSF101912; 1.
DR   PROSITE; PS51004; SEMA; 1.
PE   2: Evidence at transcript level;
KW   Adaptive immunity; Angiogenesis; Cell membrane; Developmental protein;
KW   Differentiation; Disulfide bond; Glycoprotein; Immunity;
KW   Immunoglobulin domain; Membrane; Neurogenesis; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..762
FT                   /note="Semaphorin-4A"
FT                   /id="PRO_0000239120"
FT   TOPO_DOM        33..684
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        685..705
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        706..762
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          37..495
FT                   /note="Sema"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DOMAIN          497..544
FT                   /note="PSI"
FT   DOMAIN          574..632
FT                   /note="Ig-like C2-type"
FT   REGION          722..762
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        728..762
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        121
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        136
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        314
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        497
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        608
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        114..125
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DISULFID        143..152
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DISULFID        270..380
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DISULFID        294..340
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DISULFID        498..515
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DISULFID        507..524
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
SQ   SEQUENCE   762 AA;  83627 MW;  4DFF24A64E2F3813 CRC64;
     MALPALGLDS WSFLGLFLFQ LLLLFLPPAT TAGREGQGPT PRVKYHAGDG RRALSFFHQK
     GLQDFDTLLL SDDGGTLYVG AREAILALNI EDPGVPRLKN MIPWPASDRK KSECAFKRKS
     NETQCFNFIR VLVSFNSTHL YACGTFAFSP ACTFIELQDS RLLPISEDRV VEGKGQSPFD
     PTHKHTAVMA DGMLYSGTMN NFLGSEPILL RTLGSQPVLK TDNFLRWLQP DASFVAAIPS
     TQVVYFFFEE TASEFEFFEK LRISRVAQVC KNDVGGEKLL QKKWTTFLKA QLLCTQPEQL
     PFNVIRHAVL QADNSSTDPQ VYAVFTSQWH VGGTRSSAVC AFSLKDIKSV FEGKYKELDK
     ETSRWTTYEY PDISPRPGSC SKGPSSDKAL TFMKDHFLMD EPVVGTPLLV KSGVEYTWLA
     VETAQGIDGQ SHLVMYLGTS TGSLHKAVVS GDHSAYLVEE IQLFPDPEPV RNLQLAPTQG
     AVFVGFSGGI WKVPRANCSV YESCMDCVLA RDPHCAWDPE SQTCRLLPTP ILKSWKQDMQ
     QGNPEWACAS GPMGRSLGPR SRPQIIKEVL AVPNSILELP CPQSSALASY HWSHGVEAIP
     EAPSTVYNGS LLLLLRDGAG GLYQCWATEN DFSYPVVSYW VHSQDQPLAL DPKLAGIPRE
     RMEAPLTRVG GGAALAAPKS YWPHFLTVTV LLALVLSGAL VTFLVSPLGA LRARGKVQGC
     GTLPSREKAP LSSEQCLQPS KEGRTSASDM DADNNLQGTE VA