SEM4D_CHICK
ID SEM4D_CHICK Reviewed; 295 AA.
AC Q90665;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Semaphorin-4D;
DE AltName: Full=Collapsin-4;
DE Short=COLL-4;
DE Flags: Fragment;
GN Name=SEMA4D; Synonyms=COLL4;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7605628; DOI=10.1016/0896-6273(95)90261-9;
RA Luo Y., Shepherd I., Li J., Renzi M.J., Chang S., Raper J.A.;
RT "A family of molecules related to collapsin in the embryonic chick nervous
RT system.";
RL Neuron 14:1131-1140(1995).
CC -!- FUNCTION: Cell surface receptor for PLXNB1 that plays an important role
CC in cell-cell signaling (By similarity). Regulates GABAergic synapse
CC development (By similarity). Promotes the development of inhibitory
CC synapses in a PLXNB1-dependent manner (By similarity). Modulates the
CC complexity and arborization of developing neurites in hippocampal
CC neurons by activating PLXNB1 and interaction with PLXNB1 mediates
CC activation of RHOA (By similarity). {ECO:0000250|UniProtKB:O09126,
CC ECO:0000250|UniProtKB:Q92854}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with PLXNB1 (By
CC similarity). {ECO:0000250|UniProtKB:Q92854}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q92854};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
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DR EMBL; U28242; AAA86898.1; -; mRNA.
DR RefSeq; NP_001280031.1; NM_001293102.1.
DR AlphaFoldDB; Q90665; -.
DR SMR; Q90665; -.
DR STRING; 9031.ENSGALP00000037144; -.
DR PaxDb; Q90665; -.
DR GeneID; 396331; -.
DR KEGG; gga:396331; -.
DR CTD; 10507; -.
DR VEuPathDB; HostDB:geneid_396331; -.
DR eggNOG; KOG3611; Eukaryota.
DR InParanoid; Q90665; -.
DR OrthoDB; 64683at2759; -.
DR PhylomeDB; Q90665; -.
DR Proteomes; UP000000539; 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:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0050919; P:negative chemotaxis; IBA:GO_Central.
DR GO; GO:0010693; P:negative regulation of alkaline phosphatase activity; IBA:GO_Central.
DR GO; GO:0048843; P:negative regulation of axon extension involved in axon guidance; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0001755; P:neural crest cell migration; IBA:GO_Central.
DR GO; GO:0043931; P:ossification involved in bone maturation; IBA:GO_Central.
DR GO; GO:0030335; P:positive regulation of cell migration; IBA:GO_Central.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
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 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; PF01403; Sema; 1.
DR SMART; SM00630; Sema; 1.
DR SUPFAM; SSF101912; SSF101912; 1.
DR PROSITE; PS51004; SEMA; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Developmental protein; Differentiation; Disulfide bond;
KW Glycoprotein; Membrane; Neurogenesis; Reference proteome.
FT CHAIN <1..>295
FT /note="Semaphorin-4D"
FT /id="PRO_0000176712"
FT DOMAIN <1..273
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 275..>295
FT /note="PSI"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 30..143
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 54..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 276..293
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT NON_TER 1
FT NON_TER 295
SQ SEQUENCE 295 AA; 33525 MW; 298A49414C352F0A CRC64;
DDKIYFFFTE VSVEYEFVGK LMIPRIARVC KRDQGGLRTL QKKWTSFLKA RLICTIPDKN
LIFNIINDVF TLKSPTLKEP VIYGVFTPQL NNVGLSAVCA YNLSAVEEVF SKGKYMQSAT
VEQSHTKWVR YNGEIPNPRP GACINNEARA LNYVTSLNLP DKTLQFVKDH PLMDDSVTPV
GDRPRLVKRD VKYTQIVVDR VRALNGTIYD VMFISTDQGA LHKAISYENG MHIIEETQLF
PKFEPVQTLL LSSKKSRRYL YAGSNSGVVQ SPVAFCDTYT TCFDCVLARD PYCAW