ID   SEM3C_PONAB             Reviewed;         751 AA.
AC   Q5RE75;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Semaphorin-3C;
DE   Flags: Precursor;
GN   Name=SEMA3C;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Binds to plexin family members and plays an important role in
CC       the regulation of developmental processes. Required for normal
CC       cardiovascular development during embryogenesis. Functions as
CC       attractant for growing axons, and thereby plays an important role in
CC       axon growth and axon guidance (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with PLXND1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
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DR   EMBL; CR857661; CAH89932.1; -; mRNA.
DR   RefSeq; NP_001124906.1; NM_001131434.1.
DR   AlphaFoldDB; Q5RE75; -.
DR   SMR; Q5RE75; -.
DR   STRING; 9601.ENSPPYP00000020016; -.
DR   Ensembl; ENSPPYT00000020806; ENSPPYP00000020016; ENSPPYG00000017861.
DR   GeneID; 100171774; -.
DR   KEGG; pon:100171774; -.
DR   CTD; 10512; -.
DR   eggNOG; KOG3611; Eukaryota.
DR   GeneTree; ENSGT00940000159379; -.
DR   InParanoid; Q5RE75; -.
DR   OrthoDB; 157685at2759; -.
DR   Proteomes; UP000001595; Chromosome 7.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0030215; F:semaphorin receptor binding; IEA:Ensembl.
DR   GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
DR   GO; GO:0001974; P:blood vessel remodeling; IEA:Ensembl.
DR   GO; GO:0140074; P:cardiac endothelial to mesenchymal transition; IEA:Ensembl.
DR   GO; GO:0003215; P:cardiac right ventricle morphogenesis; IEA:Ensembl.
DR   GO; GO:0060666; P:dichotomous subdivision of terminal units involved in salivary gland branching; IEA:Ensembl.
DR   GO; GO:0060174; P:limb bud formation; IEA:Ensembl.
DR   GO; GO:0001755; P:neural crest cell migration; IEA:Ensembl.
DR   GO; GO:0021915; P:neural tube development; IEA:Ensembl.
DR   GO; GO:0003148; P:outflow tract septum morphogenesis; IEA:Ensembl.
DR   GO; GO:1905312; P:positive regulation of cardiac neural crest cell migration involved in outflow tract morphogenesis; IEA:Ensembl.
DR   GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR   GO; GO:0003350; P:pulmonary myocardium development; IEA:Ensembl.
DR   GO; GO:0071526; P:semaphorin-plexin signaling pathway; IEA:Ensembl.
DR   GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
DR   Gene3D; 2.130.10.10; -; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
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; PF07679; I-set; 1.
DR   Pfam; PF01403; Sema; 1.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00423; PSI; 1.
DR   SMART; SM00630; Sema; 1.
DR   SUPFAM; SSF101912; SSF101912; 1.
DR   SUPFAM; SSF48726; SSF48726; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS51004; SEMA; 1.
PE   2: Evidence at transcript level;
KW   Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Neurogenesis; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..751
FT                   /note="Semaphorin-3C"
FT                   /id="PRO_0000345145"
FT   DOMAIN          28..511
FT                   /note="Sema"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DOMAIN          571..655
FT                   /note="Ig-like C2-type"
FT   REGION          712..751
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        714..728
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        123
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        252
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        268
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        465
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        585
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        586
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        101..112
FT                   /evidence="ECO:0000250"
FT   DISULFID        130..139
FT                   /evidence="ECO:0000250"
FT   DISULFID        266..378
FT                   /evidence="ECO:0000250"
FT   DISULFID        290..338
FT                   /evidence="ECO:0000250"
FT   DISULFID        514..532
FT                   /evidence="ECO:0000250"
FT   DISULFID        592..643
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   751 AA;  85192 MW;  4D942136BD698B69 CRC64;
     MAFRTICVLV GVFICSICVK GSSQPQARVY LTFDELRETK TSEYFSLSHH PLDYRILLMD
     EDQDRIYVGS KDHILSLNIN NISQEPLSVF WPASTIKVEE CKMAGKDPTH GCGNFVRVIQ
     TFNRTHLYVC GSGAFSPVCT YLNRGRRSED QVFMIDSKCE SGKGRCSFNP NVNTVSVMIN
     EELFSGMYID FMGTDAAIFR SLTKRNAVRT DQHNSKWLSE PMFVDAHVIP DGTDPNDAKV
     YFFFKEKLTD NNRSTKQIHS MIARICPNDT GGLRSLVNKW TTFLKARLVC SVTDEDGPET
     HFDELEDVFL LETDNPRTTL VYGIFTTSSS VFKGSAVCVY HLSDIQTVFN GPFAHKEGPN
     HQLISYQGRI PYPRPGTCPG GAFTPNMRTT KEFPDDVVTF IRNHPLMYNS IYPVHKRPLI
     VRIGTDYKYT KIAVDRVNAA DGRYHVLFLG TDRGTVQKVV VLPTNSSVSG ELILEELEVF
     KNHAPITTMK ISSKKQQLYV SSNEGVSQVS LHRCHIYGTA CADCCLARDP YCAWDGHSCS
     RFYPTGKRRS RRQDVRHGNP LTQCRGFNLK AYRNAAEIVQ YGVKNNTTFL ECAPKSPQAS
     IKWLLQKDKD RRKEVKLNER IIATSQGLLI RSVQGSDQGL YHCIATENSF KQTIAKINFK
     VLDSEMVAVV TDKWSPWTWA SSVRALPFHP KDIMGAFSHS EMQMINQYCK DTRQQHQQGD
     ESQKMRGDYG KLKALINSRK SRNRRNQLPE S