LOCUS       NP_004177                785 aa            linear   PRI 01-OCT-2024
DEFINITION  semaphorin-3F isoform 1 precursor [Homo sapiens].
ACCESSION   NP_004177
VERSION     NP_004177.3
DBSOURCE    REFSEQ: accession NM_004186.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 785)
  AUTHORS   Moragas,N., Fernandez-Nogueira,P., Recalde-Percaz,L., Inman,J.L.,
            Lopez-Plana,A., Bergholtz,H., Noguera-Castells,A., Del Burgo,P.J.,
            Chen,X., Sorlie,T., Gascon,P., Bragado,P., Bissell,M., Carbo,N. and
            Fuster,G.
  TITLE     The SEMA3F-NRP1/NRP2 axis is a key factor in the acquisition of
            invasive traits in in situ breast ductal carcinoma
  JOURNAL   Breast Cancer Res 26 (1), 122 (2024)
   PUBMED   39138514
  REMARK    GeneRIF: The SEMA3F-NRP1/NRP2 axis is a key factor in the
            acquisition of invasive traits in in situ breast ductal carcinoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 785)
  AUTHORS   Li,Q., Ma,N., Li,X., Yang,C., Zhang,W., Xiong,J., Zhu,L., Li,J.,
            Wen,Q., Gao,L., Yang,C., Rao,L., Gao,L., Zhang,X. and Rao,J.
  TITLE     Reverse effect of Semaphorin-3F on rituximab resistance in diffuse
            large B-cell lymphoma via the Hippo pathway
  JOURNAL   Chin Med J (Engl) 136 (12), 1448-1458 (2023)
   PUBMED   37114652
  REMARK    GeneRIF: Reverse effect of Semaphorin-3F on rituximab resistance in
            diffuse large B-cell lymphoma via the Hippo pathway.
REFERENCE   3  (residues 1 to 785)
  AUTHORS   Duncan,B.W., Mohan,V., Wade,S.D., Truong,Y., Kampov-Polevoi,A.,
            Temple,B.R. and Maness,P.F.
  TITLE     Semaphorin3F Drives Dendritic Spine Pruning Through Rho-GTPase
            Signaling
  JOURNAL   Mol Neurobiol 58 (8), 3817-3834 (2021)
   PUBMED   33856648
  REMARK    GeneRIF: Semaphorin3F Drives Dendritic Spine Pruning Through
            Rho-GTPase Signaling.
REFERENCE   4  (residues 1 to 785)
  AUTHORS   Halabi,R., Watterston,C., Hehr,C.L., Mori-Kreiner,R., Childs,S.J.
            and McFarlane,S.
  TITLE     Semaphorin 3fa Controls Ocular Vascularization From the Embryo
            Through to the Adult
  JOURNAL   Invest Ophthalmol Vis Sci 62 (2), 21 (2021)
   PUBMED   33595613
  REMARK    GeneRIF: Semaphorin 3fa Controls Ocular Vascularization From the
            Embryo Through to the Adult.
REFERENCE   5  (residues 1 to 785)
  AUTHORS   Xie,Z., Li,T., Huang,B., Liu,S., Zhang,L. and Zhang,Q.
  TITLE     Semaphorin 3F Serves as a Tumor Suppressor in Esophageal Squamous
            Cell Carcinoma and is Associated With Lymph Node Metastasis in
            Disease Progression
  JOURNAL   Technol Cancer Res Treat 19, 1533033820928117 (2020)
   PUBMED   32441221
  REMARK    GeneRIF: Semaphorin 3F Serves as a Tumor Suppressor in Esophageal
            Squamous Cell Carcinoma and is Associated With Lymph Node
            Metastasis in Disease Progression.
REFERENCE   6  (residues 1 to 785)
  AUTHORS   Sekido,Y., Bader,S., Latif,F., Chen,J.Y., Duh,F.M., Wei,M.H.,
            Albanesi,J.P., Lee,C.C., Lerman,M.I. and Minna,J.D.
  TITLE     Human semaphorins A(V) and IV reside in the 3p21.3 small cell lung
            cancer deletion region and demonstrate distinct expression patterns
  JOURNAL   Proc Natl Acad Sci U S A 93 (9), 4120-4125 (1996)
   PUBMED   8633026
REFERENCE   7  (residues 1 to 785)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
REFERENCE   8  (residues 1 to 785)
  AUTHORS   Goshima,Y., Nakamura,F., Strittmatter,P. and Strittmatter,S.M.
  TITLE     Collapsin-induced growth cone collapse mediated by an intracellular
            protein related to UNC-33
  JOURNAL   Nature 376 (6540), 509-514 (1995)
   PUBMED   7637782
REFERENCE   9  (residues 1 to 785)
  AUTHORS   Kolodkin,A.L., Matthes,D.J. and Goodman,C.S.
  TITLE     The semaphorin genes encode a family of transmembrane and secreted
            growth cone guidance molecules
  JOURNAL   Cell 75 (7), 1389-1399 (1993)
   PUBMED   8269517
REFERENCE   10 (residues 1 to 785)
  AUTHORS   Luo,Y., Raible,D. and Raper,J.A.
  TITLE     Collapsin: a protein in brain that induces the collapse and
            paralysis of neuronal growth cones
  JOURNAL   Cell 75 (2), 217-227 (1993)
   PUBMED   8402908
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC104450.2, BF058597.1,
            BC042914.1, AA378582.1 and CB240860.1.
            
            On May 16, 2008 this sequence version replaced NP_004177.2.
            
            Summary: This gene encodes a member of the semaphorin III family of
            secreted signaling proteins that are involved in axon guidance
            during neuronal development. The encoded protein contains an
            N-terminal Sema domain, an immunoglobulin loop and a C-terminal
            basic domain. This gene is expressed by the endothelial cells where
            it was found to act in an autocrine fashion to induce apoptosis,
            inhibit cell proliferation and survival, and function as an
            anti-tumorigenic agent. Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Jan 2016].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC042914.1, U33920.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000002829.8/ ENSP00000002829.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..785
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..785
                     /product="semaphorin-3F isoform 1 precursor"
                     /note="sema domain, immunoglobulin domain (Ig), short
                     basic domain, secreted, 3F; semaphorin III/F; semaphorin
                     IV; sema domain, immunoglobulin domain (Ig), short basic
                     domain, secreted, (semaphorin) 3F"
                     /calculated_mol_wt=86488
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1912
     mat_peptide     19..785
                     /product="Semaphorin-3F. /id=PRO_0000032320"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13275.2)"
                     /calculated_mol_wt=86488
     Region          48..548
                     /region_name="Sema_3F"
                     /note="The Sema domain, a protein interacting module, of
                     semaphorin 3F (Sema3F); cd11254"
                     /db_xref="CDD:200515"
     Site            53
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13275.2)"
     Site            order(105..108,198..199,203,224,226..227,234,244,247..248,
                     250,255,284,307..311,313,429,433,436)
                     /site_type="other"
                     /note="putative plexin binding site [polypeptide binding]"
                     /db_xref="CDD:200515"
     Site            126
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13275.2)"
     Site            order(285..287,290..292,326,329..330,332,334,338,361..368,
                     394..397,442,457)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:200515"
     Region          547..584
                     /region_name="PSI"
                     /note="domain found in Plexins, Semaphorins and Integrins;
                     smart00423"
                     /db_xref="CDD:214655"
     Region          608..697
                     /region_name="Ig_Sema3"
                     /note="Immunoglobulin (Ig)-like domain of class III
                     semaphorin Sema3; cd05871"
                     /db_xref="CDD:409455"
     Region          608..614
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409455"
     Region          619..627
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409455"
     Site            order(621,666)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:409455"
     Region          633..639
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409455"
     Region          641..644
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409455"
     Region          654..658
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409455"
     Region          661..668
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409455"
     Region          674..683
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409455"
     Region          686..697
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409455"
     Region          752..785
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13275.2)"
     CDS             1..785
                     /gene="SEMA3F"
                     /gene_synonym="SEMA-IV; SEMA4; SEMAK"
                     /coded_by="NM_004186.5:290..2647"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS2811.1"
                     /db_xref="GeneID:6405"
                     /db_xref="HGNC:HGNC:10728"
                     /db_xref="MIM:601124"
ORIGIN      
        1 mlvaglllwa slltgawpsf ptqdhlpatp rvrlsfkelk atgtahffnf llnttdyril
       61 lkdedhdrmy vgskdyvlsl dlhdinrepl iihwaaspqr ieecvlsgkd vngecgnfvr
      121 liqpwnrthl yvcgtgaynp mctyvnrgrr aqatpwtqtq avrgrgsrat dgalrpmpta
      181 prqdyifyle perlesgkgk cpydpkldta salineelya gvyidfmgtd aaifrtlgkq
      241 tamrtdqyns rwlndpsfih aelipdsaer nddklyfffr ersaeapqsp avyarigric
      301 lnddgghccl vnkwstflka rlvcsvpged giethfdelq dvfvqqtqdv rnpviyavft
      361 ssgsvfrgsa vcvysmadir mvfngpfahk egpnyqwmpf sgkmpyprpg tcpggtftps
      421 mkstkdypde vinfmrshpl myqavyplqr rplvvrtgap yrlttiavdq vdaadgryev
      481 lflgtdrgtv qkvivlpkdd qeleelmlee vevfkdpapv ktmtisskrq qlyvasavgv
      541 thlslhrcqa ygaacadccl ardpycawdg qacsrytass krrsrrqdvr hgnpirqcrg
      601 fnsnanknav esvqygvags aaflecqprs pqatvkwlfq rdpgdrrrei raedrflrte
      661 qglllralql sdrglyscta tennfkhvvt rvqlhvlgrd avhaalfppl smsappppga
      721 gpptppyqel aqllaqpevg lihqycqgyw rhvppsprea pgaprspepq dqkkprnrrh
      781 hppdt
//
