SEM7A_HUMAN
ID SEM7A_HUMAN Reviewed; 666 AA.
AC O75326; B4DDP7; F5H1S0; Q1XE81; Q1XE82; Q1XE83; Q1XE84; Q3MIY5;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Semaphorin-7A;
DE AltName: Full=CDw108;
DE AltName: Full=JMH blood group antigen;
DE AltName: Full=John-Milton-Hargen human blood group Ag;
DE AltName: Full=Semaphorin-K1;
DE Short=Sema K1;
DE AltName: Full=Semaphorin-L;
DE Short=Sema L;
DE AltName: CD_antigen=CD108;
DE Flags: Precursor;
GN Name=SEMA7A; Synonyms=CD108, SEMAL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RX PubMed=9721204; DOI=10.1006/geno.1998.5256;
RA Lange C., Liehr T., Goen M., Gebhart E., Fleckenstein B., Ensser A.;
RT "New eukaryotic semaphorins with close homology to semaphorins of DNA
RT viruses.";
RL Genomics 51:340-350(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION,
RP GLYCOSYLATION, AND TISSUE SPECIFICITY.
RX PubMed=10201933;
RA Yamada A., Kubo K., Takeshita T., Harashima N., Kawano K., Mine T.,
RA Sagawa K., Sugamura K., Itoh K.;
RT "Molecular cloning of a glycosylphosphatidylinositol-anchored molecule
RT CDw108.";
RL J. Immunol. 162:4094-4100(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=9712866; DOI=10.1074/jbc.273.35.22428;
RA Xu X., Ng S., Wu Z.-L., Nguyen D., Homburger S., Seidel-Dugan C., Ebens A.,
RA Luo Y.;
RT "Human semaphorin K1 is glycosylphosphatidylinositol-linked and defines a
RT new subfamily of viral-related semaphorins.";
RL J. Biol. Chem. 273:22428-22434(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), POLYMORPHISM, AND VARIANTS GLN-207;
RP TRP-207; HIS-460 AND CYS-461.
RC TISSUE=Peripheral blood;
RX PubMed=17207242; DOI=10.1111/j.1537-2995.2007.01076.x;
RA Seltsam A., Strigens S., Levene C., Yahalom V., Moulds M., Moulds J.J.,
RA Hustinx H., Weisbach V., Figueroa D., Bade-Doeding C., DeLuca D.S.,
RA Blasczyk R.;
RT "The molecular diversity of Sema7A, the semaphorin that carries the JMH
RT blood group antigens.";
RL Transfusion 47:133-146(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-115.
RG SeattleSNPs variation discovery resource;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain cortex;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP CHARACTERIZATION.
RX PubMed=10416131; DOI=10.1016/s0171-2985(99)80073-4;
RA Angelisova P., Drbal K., Cerny J., Hilgert I., Horejsi V.;
RT "Characterization of the human leukocyte GPI-anchored glycoprotein CDw108
RT and its relation to other similar molecules.";
RL Immunobiology 200:234-245(1999).
RN [10]
RP FUNCTION, INTERACTION WITH ITGB1, AND MUTAGENESIS OF ARG-267 AND ASP-269.
RX PubMed=12879062; DOI=10.1038/nature01790;
RA Pasterkamp R.J., Peschon J.J., Spriggs M.K., Kolodkin A.L.;
RT "Semaphorin 7A promotes axon outgrowth through integrins and MAPKs.";
RL Nature 424:398-405(2003).
RN [11]
RP FUNCTION, AND INTERACTION WITH ITGA1 AND ITGB1.
RX PubMed=17377534; DOI=10.1038/nature05652;
RA Suzuki K., Okuno T., Yamamoto M., Pasterkamp R.J., Takegahara N.,
RA Takamatsu H., Kitao T., Takagi J., Rennert P.D., Kolodkin A.L.,
RA Kumanogoh A., Kikutani H.;
RT "Semaphorin 7A initiates T-cell-mediated inflammatory responses through
RT alpha1beta1 integrin.";
RL Nature 446:680-684(2007).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ITGB1, INDUCTION, AND
RP TISSUE SPECIFICITY.
RX PubMed=17671519; DOI=10.1038/sj.jid.5700974;
RA Scott G.A., McClelland L.A., Fricke A.F.;
RT "Semaphorin 7a promotes spreading and dendricity in human melanocytes
RT through beta1-integrins.";
RL J. Invest. Dermatol. 128:151-161(2008).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 45-634 IN COMPLEX WITH PLXNC1,
RP SUBUNIT, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-105; ASN-157; ASN-258
RP AND ASN-330.
RX PubMed=20727575; DOI=10.1016/j.cell.2010.07.040;
RA Liu H., Juo Z.S., Shim A.H., Focia P.J., Chen X., Garcia K.C., He X.;
RT "Structural basis of semaphorin-plexin recognition and viral mimicry from
RT Sema7A and A39R complexes with PlexinC1.";
RL Cell 142:749-761(2010).
RN [14]
RP VARIANT LEU-347.
RX PubMed=20854351; DOI=10.1111/j.1423-0410.2010.01413.x;
RA Richard M., St-Laurent J., Perreault J., Long A., St-Louis M.;
RT "A new SEMA7A variant found in Native Americans with alloantibody.";
RL Vox Sang. 100:322-326(2011).
CC -!- FUNCTION: Plays an important role in integrin-mediated signaling and
CC functions both in regulating cell migration and immune responses.
CC Promotes formation of focal adhesion complexes, activation of the
CC protein kinase PTK2/FAK1 and subsequent phosphorylation of MAPK1 and
CC MAPK3. Promotes production of pro-inflammatory cytokines by monocytes
CC and macrophages. Plays an important role in modulating inflammation and
CC T-cell-mediated immune responses. Promotes axon growth in the embryonic
CC olfactory bulb. Promotes attachment, spreading and dendrite outgrowth
CC in melanocytes. {ECO:0000269|PubMed:12879062,
CC ECO:0000269|PubMed:17377534, ECO:0000269|PubMed:17671519}.
CC -!- SUBUNIT: Interacts with ITGA1 and ITGB1 (Probable). Interacts with
CC PLXNC1. {ECO:0000269|PubMed:12879062, ECO:0000269|PubMed:17377534,
CC ECO:0000269|PubMed:17671519, ECO:0000269|PubMed:20727575, ECO:0000305}.
CC -!- INTERACTION:
CC O75326; P16333: NCK1; NbExp=2; IntAct=EBI-1753538, EBI-389883;
CC O75326; O60486: PLXNC1; NbExp=4; IntAct=EBI-1753538, EBI-2927384;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10201933,
CC ECO:0000269|PubMed:17671519, ECO:0000269|PubMed:9712866}; Lipid-anchor,
CC GPI-anchor {ECO:0000269|PubMed:10201933, ECO:0000269|PubMed:17671519,
CC ECO:0000269|PubMed:9712866}; Extracellular side
CC {ECO:0000269|PubMed:10201933, ECO:0000269|PubMed:17671519,
CC ECO:0000269|PubMed:9712866}. Note=Detected in a punctate pattern on the
CC cell membrane of basal and supra-basal skin keratinocytes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O75326-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75326-2; Sequence=VSP_045349;
CC -!- TISSUE SPECIFICITY: Detected in skin keratinocytes and on endothelial
CC cells from skin blood vessels (at protein level). Expressed in
CC fibroblasts, keratinocytes, melanocytes, placenta, testis, ovary,
CC spleen, brain, spinal chord, lung, heart, adrenal gland, lymph nodes,
CC thymus, intestine and kidney. {ECO:0000269|PubMed:10201933,
CC ECO:0000269|PubMed:17671519, ECO:0000269|PubMed:9712866}.
CC -!- INDUCTION: Up-regulated in UV-irradiated fibroblasts, but not in UV-
CC irradiated keratinocytes. {ECO:0000269|PubMed:17671519}.
CC -!- POLYMORPHISM: Genetic variations in SEMA7A define the John Milton Hagen
CC blood group system (JMH) [MIM:614745]. Three different JMH phenotypes
CC have been identified based on the presence or absence of the high-
CC frequency JMH antigen: JMH-weak, JMH-negative, and JMH-variant. The
CC JMH-weak and -negative phenotypes can be either acquired or inherited
CC and are characterized by a reduction or complete loss of JMH expression
CC on red blood cells. Individuals with the JMH-variant phenotype are
CC usually JMH-positive and have alloantibodies compatible with JMH-
CC negative red blood cells. The JMH-variant phenotype results from rare
CC SEMA7A missense variants. {ECO:0000269|PubMed:17207242}.
CC -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene mutation
CC database;
CC URL="https://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=jmh";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/sema7a/";
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DR EMBL; AF030698; AAC34261.1; -; mRNA.
DR EMBL; AF030697; AAC34741.1; -; Genomic_DNA.
DR EMBL; AF069493; AAC82642.1; -; mRNA.
DR EMBL; AF071542; AAC80456.1; -; mRNA.
DR EMBL; AM180445; CAJ55398.1; -; mRNA.
DR EMBL; AM180446; CAJ55399.1; -; mRNA.
DR EMBL; AM180447; CAJ55400.1; -; mRNA.
DR EMBL; AM180448; CAJ55401.1; -; mRNA.
DR EMBL; AM180449; CAJ55402.1; -; mRNA.
DR EMBL; AM180450; CAJ55403.1; -; mRNA.
DR EMBL; AM180451; CAJ55404.1; -; mRNA.
DR EMBL; AK293280; BAG56808.1; -; mRNA.
DR EMBL; AY885237; AAW62253.1; -; Genomic_DNA.
DR EMBL; AC012435; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090826; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC101643; AAI01644.1; -; mRNA.
DR EMBL; BC101647; AAI01648.1; -; mRNA.
DR CCDS; CCDS10262.1; -. [O75326-1]
DR CCDS; CCDS53959.1; -. [O75326-2]
DR RefSeq; NP_001139501.1; NM_001146029.2. [O75326-2]
DR RefSeq; NP_001139502.1; NM_001146030.2.
DR RefSeq; NP_003603.1; NM_003612.4. [O75326-1]
DR PDB; 3NVQ; X-ray; 2.40 A; A/E=45-634.
DR PDBsum; 3NVQ; -.
DR AlphaFoldDB; O75326; -.
DR SMR; O75326; -.
DR BioGRID; 114056; 31.
DR CORUM; O75326; -.
DR IntAct; O75326; 23.
DR MINT; O75326; -.
DR STRING; 9606.ENSP00000261918; -.
DR GlyConnect; 1977; 7 N-Linked glycans (2 sites).
DR GlyGen; O75326; 6 sites, 7 N-linked glycans (2 sites).
DR iPTMnet; O75326; -.
DR PhosphoSitePlus; O75326; -.
DR SwissPalm; O75326; -.
DR BioMuta; SEMA7A; -.
DR EPD; O75326; -.
DR jPOST; O75326; -.
DR MassIVE; O75326; -.
DR MaxQB; O75326; -.
DR PaxDb; O75326; -.
DR PeptideAtlas; O75326; -.
DR PRIDE; O75326; -.
DR ProteomicsDB; 25743; -.
DR ProteomicsDB; 49896; -. [O75326-1]
DR Antibodypedia; 14570; 431 antibodies from 33 providers.
DR DNASU; 8482; -.
DR Ensembl; ENST00000261918.9; ENSP00000261918.4; ENSG00000138623.10. [O75326-1]
DR Ensembl; ENST00000543145.6; ENSP00000438966.2; ENSG00000138623.10. [O75326-2]
DR Ensembl; ENST00000671713.1; ENSP00000500448.1; ENSG00000288455.1. [O75326-1]
DR Ensembl; ENST00000672978.1; ENSP00000500204.1; ENSG00000288455.1. [O75326-2]
DR GeneID; 8482; -.
DR KEGG; hsa:8482; -.
DR MANE-Select; ENST00000261918.9; ENSP00000261918.4; NM_003612.5; NP_003603.1.
DR UCSC; uc002axv.4; human. [O75326-1]
DR CTD; 8482; -.
DR DisGeNET; 8482; -.
DR GeneCards; SEMA7A; -.
DR HGNC; HGNC:10741; SEMA7A.
DR HPA; ENSG00000138623; Tissue enhanced (lymphoid tissue, retina).
DR MalaCards; SEMA7A; -.
DR MIM; 607961; gene+phenotype.
DR MIM; 614745; phenotype.
DR neXtProt; NX_O75326; -.
DR OpenTargets; ENSG00000138623; -.
DR PharmGKB; PA35663; -.
DR VEuPathDB; HostDB:ENSG00000138623; -.
DR eggNOG; KOG3611; Eukaryota.
DR GeneTree; ENSGT00940000158358; -.
DR InParanoid; O75326; -.
DR OMA; GYHMGLP; -.
DR PhylomeDB; O75326; -.
DR TreeFam; TF333698; -.
DR PathwayCommons; O75326; -.
DR Reactome; R-HSA-416700; Other semaphorin interactions.
DR SignaLink; O75326; -.
DR SIGNOR; O75326; -.
DR BioGRID-ORCS; 8482; 11 hits in 1076 CRISPR screens.
DR ChiTaRS; SEMA7A; human.
DR EvolutionaryTrace; O75326; -.
DR GeneWiki; SEMA7A; -.
DR GenomeRNAi; 8482; -.
DR Pharos; O75326; Tbio.
DR PRO; PR:O75326; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; O75326; protein.
DR Bgee; ENSG00000138623; Expressed in spleen and 96 other tissues.
DR ExpressionAtlas; O75326; baseline and differential.
DR Genevisible; O75326; HS.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB.
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:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0045499; F:chemorepellent activity; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0030215; F:semaphorin receptor binding; IBA:GO_Central.
DR GO; GO:0048675; P:axon extension; IEA:Ensembl.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IDA:UniProtKB.
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:0021988; P:olfactory lobe development; IEA:Ensembl.
DR GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB.
DR GO; GO:0045773; P:positive regulation of axon extension; IDA:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IBA:GO_Central.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
DR GO; GO:0060907; P:positive regulation of macrophage cytokine production; ISS:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
DR GO; GO:0050727; P:regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; IBA:GO_Central.
DR CDD; cd11243; Sema_7A; 1.
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; IPR002165; Plexin_repeat.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR042824; Sema7A_sema.
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; PF13895; Ig_2; 1.
DR Pfam; PF01437; PSI; 1.
DR Pfam; PF01403; Sema; 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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Developmental protein;
KW Differentiation; Disulfide bond; Glycoprotein; GPI-anchor;
KW Immunoglobulin domain; Inflammatory response; Lipoprotein; Membrane;
KW Methylation; Neurogenesis; Reference proteome; Signal.
FT SIGNAL 1..44
FT /evidence="ECO:0000255"
FT CHAIN 45..648
FT /note="Semaphorin-7A"
FT /id="PRO_0000032347"
FT PROPEP 649..666
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000032348"
FT DOMAIN 53..490
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 544..629
FT /note="Ig-like C2-type"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..269
FT /note="Interaction with integrins"
FT MOTIF 267..269
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..18
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 135
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9QUR8"
FT LIPID 648
FT /note="GPI-anchor amidated alanine"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20727575"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20727575"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20727575"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20727575"
FT CARBOHYD 602
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:10201933"
FT DISULFID 120..126
FT /evidence="ECO:0000269|PubMed:20727575"
FT DISULFID 143..152
FT /evidence="ECO:0000269|PubMed:20727575"
FT DISULFID 266..366
FT /evidence="ECO:0000269|PubMed:20727575"
FT DISULFID 291..335
FT /evidence="ECO:0000269|PubMed:20727575"
FT DISULFID 493..511
FT /evidence="ECO:0000269|PubMed:20727575"
FT DISULFID 500..541
FT /evidence="ECO:0000269|PubMed:20727575"
FT DISULFID 503..518
FT /evidence="ECO:0000269|PubMed:20727575"
FT DISULFID 566..613
FT /evidence="ECO:0000269|PubMed:20727575"
FT DISULFID 587..596
FT /evidence="ECO:0000269|PubMed:20727575"
FT VAR_SEQ 111..124
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045349"
FT VARIANT 115
FT /note="S -> T (in dbSNP:rs16968733)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_029282"
FT VARIANT 207
FT /note="R -> Q (results in JMH-variant phenotype;
FT dbSNP:rs55637216)"
FT /evidence="ECO:0000269|PubMed:17207242"
FT /id="VAR_038836"
FT VARIANT 207
FT /note="R -> W (results in JMH-variant phenotype;
FT dbSNP:rs56367230)"
FT /evidence="ECO:0000269|PubMed:17207242"
FT /id="VAR_038837"
FT VARIANT 347
FT /note="R -> L (results in JMH-variant phenotype;
FT dbSNP:rs387907241)"
FT /evidence="ECO:0000269|PubMed:20854351"
FT /id="VAR_068679"
FT VARIANT 460
FT /note="R -> H (results in JMH-variant phenotype;
FT dbSNP:rs56204206)"
FT /evidence="ECO:0000269|PubMed:17207242"
FT /id="VAR_038838"
FT VARIANT 461
FT /note="R -> C (results in JMH-variant phenotype;
FT dbSNP:rs56001514)"
FT /evidence="ECO:0000269|PubMed:17207242"
FT /id="VAR_038839"
FT MUTAGEN 267
FT /note="R->K: Abolishes ITGB1-dependent enhancement of axon
FT growth; when associated with E-269."
FT /evidence="ECO:0000269|PubMed:12879062"
FT MUTAGEN 269
FT /note="D->E: Abolishes ITGB1-dependent enhancement of axon
FT growth; when associated with K-267."
FT /evidence="ECO:0000269|PubMed:12879062"
FT CONFLICT 545
FT /note="K -> E (in Ref. 5; BAG56808)"
FT /evidence="ECO:0000305"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 129..136
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:3NVQ"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 151..158
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 204..210
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 223..230
FT /evidence="ECO:0007829|PDB:3NVQ"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 239..247
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 257..266
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:3NVQ"
FT TURN 275..279
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:3NVQ"
FT TURN 294..296
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 302..309
FT /evidence="ECO:0007829|PDB:3NVQ"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 320..326
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 332..338
FT /evidence="ECO:0007829|PDB:3NVQ"
FT HELIX 339..348
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:3NVQ"
FT HELIX 375..383
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 386..389
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 394..397
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 401..406
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 408..417
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 423..431
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 436..440
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 451..456
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 467..471
FT /evidence="ECO:0007829|PDB:3NVQ"
FT TURN 472..475
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 476..480
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 482..489
FT /evidence="ECO:0007829|PDB:3NVQ"
FT HELIX 499..505
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 511..514
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 517..520
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 523..526
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 533..535
FT /evidence="ECO:0007829|PDB:3NVQ"
FT TURN 537..540
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 541..545
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 551..556
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 562..567
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 573..579
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 582..587
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 592..602
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 609..619
FT /evidence="ECO:0007829|PDB:3NVQ"
FT STRAND 621..631
FT /evidence="ECO:0007829|PDB:3NVQ"
SQ SEQUENCE 666 AA; 74824 MW; AD3ABE56B5EBE194 CRC64;
MTPPPPGRAA PSAPRARVPG PPARLGLPLR LRLLLLLWAA AASAQGHLRS GPRIFAVWKG
HVGQDRVDFG QTEPHTVLFH EPGSSSVWVG GRGKVYLFDF PEGKNASVRT VNIGSTKGSC
LDKRDCENYI TLLERRSEGL LACGTNARHP SCWNLVNGTV VPLGEMRGYA PFSPDENSLV
LFEGDEVYST IRKQEYNGKI PRFRRIRGES ELYTSDTVMQ NPQFIKATIV HQDQAYDDKI
YYFFREDNPD KNPEAPLNVS RVAQLCRGDQ GGESSLSVSK WNTFLKAMLV CSDAATNKNF
NRLQDVFLLP DPSGQWRDTR VYGVFSNPWN YSAVCVYSLG DIDKVFRTSS LKGYHSSLPN
PRPGKCLPDQ QPIPTETFQV ADRHPEVAQR VEPMGPLKTP LFHSKYHYQK VAVHRMQASH
GETFHVLYLT TDRGTIHKVV EPGEQEHSFA FNIMEIQPFR RAAAIQTMSL DAERRKLYVS
SQWEVSQVPL DLCEVYGGGC HGCLMSRDPY CGWDQGRCIS IYSSERSVLQ SINPAEPHKE
CPNPKPDKAP LQKVSLAPNS RYYLSCPMES RHATYSWRHK ENVEQSCEPG HQSPNCILFI
ENLTAQQYGH YFCEAQEGSY FREAQHWQLL PEDGIMAEHL LGHACALAAS LWLGVLPTLT
LGLLVH
