ID   SEM3D_HUMAN             Reviewed;         777 AA.
AC   O95025; A6NK46; Q6UW77; Q8NCQ1;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   13-FEB-2019, entry version 156.
DE   RecName: Full=Semaphorin-3D;
DE   Flags: Precursor;
GN   Name=SEMA3D; ORFNames=UNQ760/PRO1491;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-701.
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
RA   Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA   Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA   Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA   Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA   Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA   Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale
RT   effort to identify novel human secreted and transmembrane proteins: a
RT   bioinformatics assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA   Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA   Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA   Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA   Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA   Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA   Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA   Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA   Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA   Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA   Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA   Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA   Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA   Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA   Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA   Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA   Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA   Waterston R.H., Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 327-777.
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Induces the collapse and paralysis of neuronal growth
CC       cones. Could potentially act as repulsive cues toward specific
CC       neuronal populations. Binds to neuropilin (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- DOMAIN: Strong binding to neuropilin is mediated by the carboxy
CC       third of the protein.
CC   -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH29590.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AY358937; AAQ89296.1; -; mRNA.
DR   EMBL; AC004957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC029590; AAH29590.1; ALT_INIT; mRNA.
DR   CCDS; CCDS34676.1; -.
DR   RefSeq; NP_689967.2; NM_152754.2.
DR   RefSeq; XP_011514262.1; XM_011515960.1.
DR   RefSeq; XP_016867362.1; XM_017011873.1.
DR   UniGene; Hs.201340; -.
DR   UniGene; Hs.664064; -.
DR   ProteinModelPortal; O95025; -.
DR   SMR; O95025; -.
DR   BioGrid; 128826; 1.
DR   IntAct; O95025; 1.
DR   STRING; 9606.ENSP00000284136; -.
DR   iPTMnet; O95025; -.
DR   PhosphoSitePlus; O95025; -.
DR   BioMuta; SEMA3D; -.
DR   EPD; O95025; -.
DR   jPOST; O95025; -.
DR   PaxDb; O95025; -.
DR   PeptideAtlas; O95025; -.
DR   PRIDE; O95025; -.
DR   ProteomicsDB; 50626; -.
DR   DNASU; 223117; -.
DR   Ensembl; ENST00000284136; ENSP00000284136; ENSG00000153993.
DR   GeneID; 223117; -.
DR   KEGG; hsa:223117; -.
DR   UCSC; uc003uic.4; human.
DR   CTD; 223117; -.
DR   DisGeNET; 223117; -.
DR   EuPathDB; HostDB:ENSG00000153993.13; -.
DR   GeneCards; SEMA3D; -.
DR   H-InvDB; HIX0006812; -.
DR   HGNC; HGNC:10726; SEMA3D.
DR   HPA; HPA037522; -.
DR   MalaCards; SEMA3D; -.
DR   MIM; 609907; gene.
DR   neXtProt; NX_O95025; -.
DR   OpenTargets; ENSG00000153993; -.
DR   Orphanet; 388; Hirschsprung disease.
DR   PharmGKB; PA35648; -.
DR   eggNOG; KOG3611; Eukaryota.
DR   eggNOG; ENOG410XQZC; LUCA.
DR   GeneTree; ENSGT00940000156681; -.
DR   HOGENOM; HOG000039964; -.
DR   HOVERGEN; HBG055071; -.
DR   InParanoid; O95025; -.
DR   KO; K06840; -.
DR   OMA; WKHVQEM; -.
DR   OrthoDB; 297290at2759; -.
DR   PhylomeDB; O95025; -.
DR   TreeFam; TF316102; -.
DR   ChiTaRS; SEMA3D; human.
DR   GenomeRNAi; 223117; -.
DR   PRO; PR:O95025; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   Bgee; ENSG00000153993; Expressed in 121 organ(s), highest expression level in tendon of biceps brachii.
DR   ExpressionAtlas; O95025; baseline and differential.
DR   Genevisible; O95025; HS.
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:0038191; F:neuropilin binding; IBA:GO_Central.
DR   GO; GO:0030215; F:semaphorin receptor binding; 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: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; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
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; 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   Complete proteome; Developmental protein; Differentiation;
KW   Disulfide bond; Glycoprotein; Immunoglobulin domain; Neurogenesis;
KW   Polymorphism; Reference proteome; Secreted; Signal.
FT   SIGNAL        1     36       {ECO:0000255}.
FT   CHAIN        37    777       Semaphorin-3D.
FT                                /FTId=PRO_0000032314.
FT   DOMAIN       44    531       Sema. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00352}.
FT   DOMAIN      533    585       PSI.
FT   DOMAIN      592    680       Ig-like C2-type.
FT   COMPBIAS    739    773       Arg/Lys-rich (basic).
FT   CARBOHYD    139    139       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    607    607       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    724    724       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    117    128       {ECO:0000250}.
FT   DISULFID    146    155       {ECO:0000250}.
FT   DISULFID    286    398       {ECO:0000250}.
FT   DISULFID    310    358       {ECO:0000250}.
FT   DISULFID    534    552       {ECO:0000250}.
FT   DISULFID    665    731       {ECO:0000250}.
FT   VARIANT     701    701       K -> Q (in dbSNP:rs7800072).
FT                                {ECO:0000269|PubMed:12975309}.
FT                                /FTId=VAR_021513.
SQ   SEQUENCE   777 AA;  89651 MW;  3F7B0D7AF50F53BD CRC64;
     MNANKDERLK ARSQDFHLFP ALMMLSMTML FLPVTGTLKQ NIPRLKLTYK DLLLSNSCIP
     FLGSSEGLDF QTLLLDEERG RLLLGAKDHI FLLSLVDLNK NFKKIYWPAA KERVELCKLA
     GKDANTECAN FIRVLQPYNK THIYVCGTGA FHPICGYIDL GVYKEDIIFK LDTHNLESGR
     LKCPFDPQQP FASVMTDEYL YSGTASDFLG KDTAFTRSLG PTHDHHYIRT DISEHYWLNG
     AKFIGTFFIP DTYNPDDDKI YFFFRESSQE GSTSDKTILS RVGRVCKNDV GGQRSLINKW
     TTFLKARLIC SIPGSDGADT YFDELQDIYL LPTRDERNPV VYGVFTTTSS IFKGSAVCVY
     SMADIRAVFN GPYAHKESAD HRWVQYDGRI PYPRPGTCPS KTYDPLIKST RDFPDDVISF
     IKRHSVMYKS VYPVAGGPTF KRINVDYRLT QIVVDHVIAE DGQYDVMFLG TDIGTVLKVV
     SISKEKWNME EVVLEELQIF KHSSIILNME LSLKQQQLYI GSRDGLVQLS LHRCDTYGKA
     CADCCLARDP YCAWDGNACS RYAPTSKRRA RRQDVKYGDP ITQCWDIEDS ISHETADEKV
     IFGIEFNSTF LECIPKSQQA TIKWYIQRSG DEHREELKPD ERIIKTEYGL LIRSLQKKDS
     GMYYCKAQEH TFIHTIVKLT LNVIENEQME NTQRAEHEEG KVKDLLAESR LRYKDYIQIL
     SSPNFSLDQY CEQMWHREKR RQRNKGGPKW KHMQEMKKKR NRRHHRDLDE LPRAVAT
//