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Database: UniProt
Entry: M3YAQ5_MUSPF
LinkDB: M3YAQ5_MUSPF
Original site: M3YAQ5_MUSPF 
ID   M3YAQ5_MUSPF            Unreviewed;       857 AA.
AC   M3YAQ5;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=Semaphorin 4D {ECO:0000313|Ensembl:ENSMPUP00000008412.1};
DE   SubName: Full=Semaphorin-4D isoform X2 {ECO:0000313|RefSeq:XP_012904586.1};
GN   Name=SEMA4D {ECO:0000313|Ensembl:ENSMPUP00000008412.1,
GN   ECO:0000313|RefSeq:XP_012904586.1};
OS   Mustela putorius furo (European domestic ferret) (Mustela furo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Mustelinae; Mustela.
OX   NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000008412.1};
RN   [1] {ECO:0000313|Ensembl:ENSMPUP00000008412.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2023) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_012904586.1}
RP   IDENTIFICATION.
RC   TISSUE=Brain {ECO:0000313|RefSeq:XP_012904586.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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; AEYP01095461; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01095462; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01095463; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01095464; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_012904586.1; XM_013049132.2.
DR   STRING; 9669.ENSMPUP00000008412; -.
DR   Ensembl; ENSMPUT00000008547.1; ENSMPUP00000008412.1; ENSMPUG00000008476.1.
DR   GeneID; 101674605; -.
DR   KEGG; mpuf:101674605; -.
DR   CTD; 10507; -.
DR   eggNOG; KOG3611; Eukaryota.
DR   GeneTree; ENSGT00940000159594; -.
DR   HOGENOM; CLU_009051_4_0_1; -.
DR   OMA; PCLKFRS; -.
DR   OrthoDB; 5342713at2759; -.
DR   Proteomes; UP000000715; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0002116; C:semaphorin receptor complex; IEA:Ensembl.
DR   GO; GO:0048018; F:receptor ligand activity; IEA:Ensembl.
DR   GO; GO:0030215; F:semaphorin receptor binding; IEA:Ensembl.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:Ensembl.
DR   GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
DR   GO; GO:0061430; P:bone trabecula morphogenesis; IEA:Ensembl.
DR   GO; GO:0070486; P:leukocyte aggregation; IEA:Ensembl.
DR   GO; GO:0007162; P:negative regulation of cell adhesion; IEA:Ensembl.
DR   GO; GO:0045668; P:negative regulation of osteoblast differentiation; IEA:Ensembl.
DR   GO; GO:0050732; P:negative regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0043931; P:ossification involved in bone maturation; IEA:Ensembl.
DR   GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR   GO; GO:0048672; P:positive regulation of collateral sprouting; IEA:Ensembl.
DR   GO; GO:1905704; P:positive regulation of inhibitory synapse assembly; IEA:Ensembl.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR   GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IEA:Ensembl.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
DR   GO; GO:0048814; P:regulation of dendrite morphogenesis; IEA:Ensembl.
DR   GO; GO:0071526; P:semaphorin-plexin signaling pathway; IEA:Ensembl.
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; IPR013151; Immunoglobulin.
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; 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   3: Inferred from homology;
KW   Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW   Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Neurogenesis {ECO:0000256|ARBA:ARBA00022902};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000715};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..857
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5041199591"
FT   TRANSMEM        730..751
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          17..498
FT                   /note="Sema"
FT                   /evidence="ECO:0000259|PROSITE:PS51004"
FT   DOMAIN          552..634
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   REGION          647..677
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          791..840
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        818..840
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   857 AA;  94999 MW;  51CC33D855F2AD1C CRC64;
     MCAPVGGLLA ALAMVLGMAV AFAPKPRITW EHREVHLEKF HEPGIFNYSV LLLSEDKTTL
     YVGAREAVFA LSAHNVSEKQ HEAYWKVSED KKAKCAEKGK SRQTECLNYI RVLQPLGPGA
     LYVCGTNAFQ PACDHLDLTS FRFLGRREDG KGRCPFDPAQ SYTSVMVDGE LYSGTSYNFL
     GSEPIISRNS SHSPLRTEYA IPWLNEPSFV FADVMRERPD GLDSGDDRVY FFFTEVSVEY
     EFVFKLMIPR VARVCKGDQG GLRTLQKKWT SFLKARLICS RPDSNLVFNV LQDVFVLRAE
     GLKEPVIYGV FTPQLNNVGL SAVCAYHLSA AEEVFSRGKY MQSTTVEQSH TKWVRYNGAV
     PTPRPGACIT REARAANLSS SLSLPDKTLQ FVKDHPLMDS SVTPIDNRPR LIRSDVNYTQ
     VVVDRTWALD GTPYDVMFVG TDQGTLHKAV SLENEAHIIE ETRLFQDLEP VQTLLLNSQK
     GRKFVYAGSS SGVVQAPVAF CEKHATCEDC VLARDPYCAW SPASQACVAL HLPDSPSRDL
     IQRMSGDTAG CPNKTKESFR QHFFKHGGTA ELKCSPKSNL ARVVWTFQNN ELKAEGPKYS
     LVGRKDLLVF NLSEGDSGVY RCLLEERLRN RTVLHVAARH VLEVRVPPRT PAAPTTPAEG
     DRTPLRVSAE PTPGPPAQTP VVLGPALGAM APPPSPTPSS TPCKPKTVVN TVPQVHSEKT
     VYLKSSDNRL LMVLFLLCFV LCLGLLSYNC YKGYLPGQCL KFRSAVLLAK KQPAADFSEF
     EQSVKETLVE QGSFSQQNGA QPRPALDTGY ETEQDTTASR APTDREDSQR LDDLPGRDRP
     FDVKCELKYA DSDADVD
//
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