ID   Q4LE41_HUMAN            Unreviewed;       870 AA.
AC   Q4LE41;
DT   02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT   02-AUG-2005, sequence version 1.
DT   02-SEP-2026, entry version 101.
DE   RecName: Full=Semaphorin-4D {ECO:0000256|ARBA:ARBA00074138};
DE   Flags: Fragment;
GN   Name=SEMA4D variant protein {ECO:0000313|EMBL:BAE06112.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:BAE06112.1};
RN   [1] {ECO:0000313|EMBL:BAE06112.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:BAE06112.1};
RA   Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R.,
RA   Okazaki N., Koga H., Nagase T., Ohara O.;
RT   "Preparation of a set of expression-ready clones of mammalian long cDNAs
RT   encoding large proteins by the ORF trap cloning method.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell surface receptor for PLXNB1 and PLXNB2 that plays an
CC       important role in cell-cell signaling. Regulates GABAergic synapse
CC       development. Promotes the development of inhibitory synapses in a
CC       PLXNB1-dependent manner. Modulates the complexity and arborization of
CC       developing neurites in hippocampal neurons by activating PLXNB1 and
CC       interaction with PLXNB1 mediates activation of RHOA. Promotes the
CC       migration of cerebellar granule cells. Plays a role in the immune
CC       system; induces B-cells to aggregate and improves their viability (in
CC       vitro). Induces endothelial cell migration through the activation of
CC       PTK2B/PYK2, SRC, and the phosphatidylinositol 3-kinase-AKT pathway.
CC       {ECO:0000256|ARBA:ARBA00058816}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC       Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the semaphorin family.
CC       {ECO:0000256|ARBA:ARBA00009492}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00352}.
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DR   EMBL; AB210030; BAE06112.1; -; mRNA.
DR   AlphaFoldDB; Q4LE41; -.
DR   PeptideAtlas; Q4LE41; -.
DR   ChiTaRS; SEMA4D; human.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030215; F:semaphorin receptor binding; IEA:InterPro.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:UniProtKB-ARBA.
DR   GO; GO:0043931; P:ossification involved in bone maturation; IEA:UniProtKB-ARBA.
DR   GO; GO:0050772; P:positive regulation of axonogenesis; IEA:UniProtKB-ARBA.
DR   GO; GO:0030335; P:positive regulation of cell migration; IEA:UniProtKB-ARBA.
DR   GO; GO:1902533; P:positive regulation of intracellular signal transduction; IEA:UniProtKB-ARBA.
DR   GO; GO:0071526; P:semaphorin-plexin signaling pathway; IEA:UniProtKB-ARBA.
DR   CDD; cd05873; Ig_Sema4D_like; 1.
DR   CDD; cd11259; Sema_4D; 1.
DR   FunFam; 2.130.10.10:FF:000120; Semaphorin 4D; 1.
DR   FunFam; 3.30.1680.10:FF:000013; Semaphorin 4D; 1.
DR   FunFam; 2.60.40.10:FF:000647; Semaphorin-4D; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 3.30.1680.10; ligand-binding face of the semaphorins, domain 2; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
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   InterPro; IPR013151; Immunoglobulin_dom.
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; SEMAPHORIN; 1.
DR   PANTHER; PTHR11036:SF18; SEMAPHORIN-4D; 1.
DR   Pfam; PF00047; ig; 1.
DR   Pfam; PF01437; PSI; 1.
DR   Pfam; PF01403; Sema; 1.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00408; IGc2; 1.
DR   SMART; SM00423; PSI; 1.
DR   SMART; SM00630; Sema; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   SUPFAM; SSF103575; Plexin repeat; 1.
DR   SUPFAM; SSF101912; Sema domain; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS51004; SEMA; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW   Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319, ECO:0000256|PROSITE-
KW   ProRule:PRU00114};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Neurogenesis {ECO:0000256|ARBA:ARBA00022902};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        743..764
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          27..508
FT                   /note="Sema"
FT                   /evidence="ECO:0000259|PROSITE:PS51004"
FT   DOMAIN          562..644
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   REGION          802..845
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        835..845
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAE06112.1"
SQ   SEQUENCE   870 AA;  97153 MW;  82999474AEEE440F CRC64;
     SPWGRLYLMR MCTPIRGLLM ALAVMFGTAM AFAPIPRITW EHREVHLVQF HEPDIYNYSA
     LLLSEDKDTL YIGAREAVFA VNALNISEKQ HEVYWKVSED KKAKCAEKGK SKQTECLNYI
     RVLQPLSATS LYVCGTNAFQ PACDHLNLTS FKFLGKNEDG KGRCPFDPAH SYTSVMVDGE
     LYSGTSYNFL GSEPIISRNS SHSPLRTEYA IPWLNEPSFV FADVIRKSPD SPDGEDDRVY
     FFFTEVSVEY EFVFRVLIPR IARVCKGDQG GLRTLQKKWT SFLKARLICS RPDSGLVFNV
     LRDVFVLRSP GLKVPVFYAL FTPQLNNVGL SAVCTYNLST AEEVFSHGKY MQSTTVEQSH
     TKWVRYNGPV PKPRPGACID SEARAANYTS SLNLPDKTLQ FVKDHPLMDD SVTPIDNRPR
     LIKKDVNYTQ IVVDRTQALD GTVYDVMFVS TDRGALHKAI SLEHAVHIIE ETQLFQDFEP
     VQTLLLSSKK GNRFVYAGSN SGVVQAPLAF CGKHGTCEDC VLARDPYCAW SPPTATCVAL
     HQTESPSRGL IQEMSGDASV CPDKSKGSYR QHFFKHGGTA ELKCSQKSNL ARVFWKFQNG
     VLKAESPKYG LMGRKNLLIF NLSEGDSGVY QCLSEERVKN KTVFQVVAKH VLEVKVVPKP
     VVAPTLSVVQ TEGSRIATKV LVASTQGSSP PTPAVQATSS GAITLPPKPA PTGTSCEPKI
     VINTVPQLHS EKTMYLKSSD NRLLMSLFLF FFVLFLCLFF YNCYKGYLPR QCLKFRSALL
     IGKKKPKSDF CDREQSLKET LVEPGSFSQQ NGEHPKPALD TGYETEQDTI TSKVPTDRED
     SQRIDDLSAR DKPFDVKCEL KFADSDADGD
//