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Semaphorin-7A (CDw108) (JMH blood group antigen) (John-Milton-Hargen human blood group Ag) (Semaphorin-K1) (Sema K1) (Semaphorin-L) (Sema L) (CD antigen CD108)

 SEM7A_HUMAN             Reviewed;         666 AA.
O75326; B4DDP7; F5H1S0; Q1XE81; Q1XE82; Q1XE83; Q1XE84; Q3MIY5;
20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
12-SEP-2018, entry version 170.
RecName: Full=Semaphorin-7A;
AltName: Full=CDw108;
AltName: Full=JMH blood group antigen;
AltName: Full=John-Milton-Hargen human blood group Ag;
AltName: Full=Semaphorin-K1;
Short=Sema K1;
AltName: Full=Semaphorin-L;
Short=Sema L;
AltName: CD_antigen=CD108;
Flags: Precursor;
Name=SEMA7A; Synonyms=CD108, SEMAL;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
PubMed=9721204; DOI=10.1006/geno.1998.5256;
Lange C., Liehr T., Goen M., Gebhart E., Fleckenstein B., Ensser A.;
"New eukaryotic semaphorins with close homology to semaphorins of DNA
viruses.";
Genomics 51:340-350(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION,
GLYCOSYLATION, AND TISSUE SPECIFICITY.
PubMed=10201933;
Yamada A., Kubo K., Takeshita T., Harashima N., Kawano K., Mine T.,
Sagawa K., Sugamura K., Itoh K.;
"Molecular cloning of a glycosylphosphatidylinositol-anchored molecule
CDw108.";
J. Immunol. 162:4094-4100(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
TISSUE=Placenta;
PubMed=9712866; DOI=10.1074/jbc.273.35.22428;
Xu X., Ng S., Wu Z.-L., Nguyen D., Homburger S., Seidel-Dugan C.,
Ebens A., Luo Y.;
"Human semaphorin K1 is glycosylphosphatidylinositol-linked and
defines a new subfamily of viral-related semaphorins.";
J. Biol. Chem. 273:22428-22434(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), POLYMORPHISM, AND VARIANTS
GLN-207; TRP-207; HIS-460 AND CYS-461.
TISSUE=Peripheral blood;
PubMed=17207242; DOI=10.1111/j.1537-2995.2007.01076.x;
Seltsam A., Strigens S., Levene C., Yahalom V., Moulds M.,
Moulds J.J., Hustinx H., Weisbach V., Figueroa D., Bade-Doeding C.,
DeLuca D.S., Blasczyk R.;
"The molecular diversity of Sema7A, the semaphorin that carries the
JMH blood group antigens.";
Transfusion 47:133-146(2007).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-115.
SeattleSNPs variation discovery resource;
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human
chromosome 15.";
Nature 440:671-675(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain cortex;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
CHARACTERIZATION.
PubMed=10416131;
Angelisova P., Drbal K., Cerny J., Hilgert I., Horejsi V.;
"Characterization of the human leukocyte GPI-anchored glycoprotein
CDw108 and its relation to other similar molecules.";
Immunobiology 200:234-245(1999).
[10]
FUNCTION, INTERACTION WITH ITGB1, AND MUTAGENESIS OF ARG-267 AND
ASP-269.
PubMed=12879062; DOI=10.1038/nature01790;
Pasterkamp R.J., Peschon J.J., Spriggs M.K., Kolodkin A.L.;
"Semaphorin 7A promotes axon outgrowth through integrins and MAPKs.";
Nature 424:398-405(2003).
[11]
FUNCTION, AND INTERACTION WITH ITGA1 AND ITGB1.
PubMed=17377534; DOI=10.1038/nature05652;
Suzuki K., Okuno T., Yamamoto M., Pasterkamp R.J., Takegahara N.,
Takamatsu H., Kitao T., Takagi J., Rennert P.D., Kolodkin A.L.,
Kumanogoh A., Kikutani H.;
"Semaphorin 7A initiates T-cell-mediated inflammatory responses
through alpha1beta1 integrin.";
Nature 446:680-684(2007).
[12]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ITGB1, INDUCTION, AND
TISSUE SPECIFICITY.
PubMed=17671519; DOI=10.1038/sj.jid.5700974;
Scott G.A., McClelland L.A., Fricke A.F.;
"Semaphorin 7a promotes spreading and dendricity in human melanocytes
through beta1-integrins.";
J. Invest. Dermatol. 128:151-161(2008).
[13]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 45-634 IN COMPLEX WITH
PLXNC1, SUBUNIT, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-105;
ASN-157; ASN-258 AND ASN-330.
PubMed=20727575; DOI=10.1016/j.cell.2010.07.040;
Liu H., Juo Z.S., Shim A.H., Focia P.J., Chen X., Garcia K.C., He X.;
"Structural basis of semaphorin-plexin recognition and viral mimicry
from Sema7A and A39R complexes with PlexinC1.";
Cell 142:749-761(2010).
[14]
VARIANT LEU-347.
PubMed=20854351; DOI=10.1111/j.1423-0410.2010.01413.x;
Richard M., St-Laurent J., Perreault J., Long A., St-Louis M.;
"A new SEMA7A variant found in Native Americans with alloantibody.";
Vox Sang. 100:322-326(2011).
-!- FUNCTION: Plays an important role in integrin-mediated signaling
and functions both in regulating cell migration and immune
responses. Promotes formation of focal adhesion complexes,
activation of the protein kinase PTK2/FAK1 and subsequent
phosphorylation of MAPK1 and MAPK3. Promotes production of
proinflammatory cytokines by monocytes and macrophages. Plays an
important role in modulating inflammation and T-cell-mediated
immune responses. Promotes axon growth in the embryonic olfactory
bulb. Promotes attachment, spreading and dendrite outgrowth in
melanocytes. {ECO:0000269|PubMed:12879062,
ECO:0000269|PubMed:17377534, ECO:0000269|PubMed:17671519}.
-!- SUBUNIT: Interacts with ITGA1 and ITGB1 (Probable). Interacts with
PLXNC1. {ECO:0000269|PubMed:12879062, ECO:0000269|PubMed:17377534,
ECO:0000269|PubMed:17671519, ECO:0000269|PubMed:20727575,
ECO:0000305}.
-!- INTERACTION:
P16333:NCK1; NbExp=2; IntAct=EBI-1753538, EBI-389883;
O60486:PLXNC1; NbExp=4; IntAct=EBI-1753538, EBI-2927384;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10201933,
ECO:0000269|PubMed:17671519, ECO:0000269|PubMed:9712866}; Lipid-
anchor, GPI-anchor {ECO:0000269|PubMed:10201933,
ECO:0000269|PubMed:17671519, ECO:0000269|PubMed:9712866};
Extracellular side {ECO:0000269|PubMed:10201933,
ECO:0000269|PubMed:17671519, ECO:0000269|PubMed:9712866}.
Note=Detected in a punctate pattern on the cell membrane of basal
and supra-basal skin keratinocytes.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O75326-1; Sequence=Displayed;
Name=2;
IsoId=O75326-2; Sequence=VSP_045349;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Detected in skin keratinocytes and on
endothelial cells from skin blood vessels (at protein level).
Expressed in fibroblasts, keratinocytes, melanocytes, placenta,
testis, ovary, spleen, brain, spinal chord, lung, heart, adrenal
gland, lymph nodes, thymus, intestine and kidney.
{ECO:0000269|PubMed:10201933, ECO:0000269|PubMed:17671519,
ECO:0000269|PubMed:9712866}.
-!- INDUCTION: Up-regulated in UV-irradiated fibroblasts, but not in
UV-irradiated keratinocytes. {ECO:0000269|PubMed:17671519}.
-!- POLYMORPHISM: Genetic variations in SEMA7A define the John Milton
Hagen blood group system (JMH) [MIM:614745]. Three different JMH
phenotypes have been identified based on the presence or absence
of the high-frequency JMH antigen: JMH-weak, JMH-negative, and
JMH-variant. The JMH-weak and -negative phenotypes can be either
acquired or inherited and are characterized by a reduction or
complete loss of JMH expression on red blood cells. Individuals
with the JMH-variant phenotype are usually JMH-positive and have
alloantibodies compatible with JMH-negative red blood cells. The
JMH-variant phenotype results from rare SEMA7A missense variants.
{ECO:0000269|PubMed:17207242}.
-!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
-!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene
mutation database;
URL="https://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=jmh";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/sema7a/";
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EMBL; AF030698; AAC34261.1; -; mRNA.
EMBL; AF030697; AAC34741.1; -; Genomic_DNA.
EMBL; AF069493; AAC82642.1; -; mRNA.
EMBL; AF071542; AAC80456.1; -; mRNA.
EMBL; AM180445; CAJ55398.1; -; mRNA.
EMBL; AM180446; CAJ55399.1; -; mRNA.
EMBL; AM180447; CAJ55400.1; -; mRNA.
EMBL; AM180448; CAJ55401.1; -; mRNA.
EMBL; AM180449; CAJ55402.1; -; mRNA.
EMBL; AM180450; CAJ55403.1; -; mRNA.
EMBL; AM180451; CAJ55404.1; -; mRNA.
EMBL; AK293280; BAG56808.1; -; mRNA.
EMBL; AY885237; AAW62253.1; -; Genomic_DNA.
EMBL; AC012435; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC090826; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC101643; AAI01644.1; -; mRNA.
EMBL; BC101647; AAI01648.1; -; mRNA.
CCDS; CCDS10262.1; -. [O75326-1]
CCDS; CCDS53959.1; -. [O75326-2]
RefSeq; NP_001139501.1; NM_001146029.2. [O75326-2]
RefSeq; NP_001139502.1; NM_001146030.2.
RefSeq; NP_003603.1; NM_003612.4. [O75326-1]
UniGene; Hs.24640; -.
PDB; 3NVQ; X-ray; 2.40 A; A/E=45-634.
PDBsum; 3NVQ; -.
ProteinModelPortal; O75326; -.
SMR; O75326; -.
BioGrid; 114056; 16.
CORUM; O75326; -.
IntAct; O75326; 7.
MINT; O75326; -.
STRING; 9606.ENSP00000261918; -.
iPTMnet; O75326; -.
PhosphoSitePlus; O75326; -.
SwissPalm; O75326; -.
BioMuta; SEMA7A; -.
EPD; O75326; -.
MaxQB; O75326; -.
PaxDb; O75326; -.
PeptideAtlas; O75326; -.
PRIDE; O75326; -.
ProteomicsDB; 49896; -.
Ensembl; ENST00000261918; ENSP00000261918; ENSG00000138623. [O75326-1]
Ensembl; ENST00000543145; ENSP00000438966; ENSG00000138623. [O75326-2]
GeneID; 8482; -.
KEGG; hsa:8482; -.
UCSC; uc002axv.4; human. [O75326-1]
CTD; 8482; -.
DisGeNET; 8482; -.
EuPathDB; HostDB:ENSG00000138623.9; -.
GeneCards; SEMA7A; -.
HGNC; HGNC:10741; SEMA7A.
HPA; HPA008210; -.
HPA; HPA042273; -.
MalaCards; SEMA7A; -.
MIM; 607961; gene+phenotype.
MIM; 614745; phenotype.
neXtProt; NX_O75326; -.
OpenTargets; ENSG00000138623; -.
PharmGKB; PA35663; -.
eggNOG; KOG3611; Eukaryota.
eggNOG; ENOG410XQZC; LUCA.
GeneTree; ENSGT00760000119134; -.
HOGENOM; HOG000154284; -.
HOVERGEN; HBG079171; -.
InParanoid; O75326; -.
KO; K06529; -.
OMA; GCHGCLM; -.
OrthoDB; EOG091G01W0; -.
PhylomeDB; O75326; -.
TreeFam; TF333698; -.
Reactome; R-HSA-416700; Other semaphorin interactions.
SIGNOR; O75326; -.
ChiTaRS; SEMA7A; human.
EvolutionaryTrace; O75326; -.
GeneWiki; SEMA7A; -.
GenomeRNAi; 8482; -.
PRO; PR:O75326; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000138623; Expressed in 195 organ(s), highest expression level in C1 segment of cervical spinal cord.
CleanEx; HS_SEMA7A; -.
ExpressionAtlas; O75326; baseline and differential.
Genevisible; O75326; HS.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005178; F:integrin binding; IBA:GO_Central.
GO; GO:0038191; F:neuropilin binding; IBA:GO_Central.
GO; GO:0048675; P:axon extension; IEA:Ensembl.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0007229; P:integrin-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0050919; P:negative chemotaxis; IBA:GO_Central.
GO; GO:0021988; P:olfactory lobe development; IEA:Ensembl.
GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB.
GO; GO:0045773; P:positive regulation of axon extension; IDA:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
GO; GO:0060907; P:positive regulation of macrophage cytokine production; ISS:UniProtKB.
GO; GO:0050727; P:regulation of inflammatory response; ISS:UniProtKB.
Gene3D; 2.130.10.10; -; 1.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR002165; Plexin_repeat.
InterPro; IPR016201; PSI.
InterPro; IPR001627; Semap_dom.
InterPro; IPR036352; Semap_dom_sf.
InterPro; IPR027231; Semaphorin.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
PANTHER; PTHR11036; PTHR11036; 1.
Pfam; PF13895; Ig_2; 1.
Pfam; PF01437; PSI; 1.
Pfam; PF01403; Sema; 1.
SMART; SM00423; PSI; 1.
SMART; SM00630; Sema; 1.
SUPFAM; SSF101912; SSF101912; 1.
SUPFAM; SSF48726; SSF48726; 1.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS51004; SEMA; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
GPI-anchor; Immunoglobulin domain; Inflammatory response; Lipoprotein;
Membrane; Methylation; Neurogenesis; Polymorphism; Reference proteome;
Signal.
SIGNAL 1 44 {ECO:0000255}.
CHAIN 45 648 Semaphorin-7A.
/FTId=PRO_0000032347.
PROPEP 649 666 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000032348.
DOMAIN 53 490 Sema. {ECO:0000255|PROSITE-
ProRule:PRU00352}.
DOMAIN 544 629 Ig-like C2-type.
REGION 267 269 Interaction with integrins.
MOTIF 267 269 Cell attachment site. {ECO:0000255}.
MOD_RES 135 135 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q9QUR8}.
LIPID 648 648 GPI-anchor amidated alanine.
{ECO:0000255}.
CARBOHYD 105 105 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20727575}.
CARBOHYD 157 157 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20727575}.
CARBOHYD 258 258 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20727575}.
CARBOHYD 330 330 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20727575}.
CARBOHYD 602 602 N-linked (GlcNAc...) asparagine.
{ECO:0000305|PubMed:10201933}.
DISULFID 120 126 {ECO:0000269|PubMed:20727575}.
DISULFID 143 152 {ECO:0000269|PubMed:20727575}.
DISULFID 266 366 {ECO:0000269|PubMed:20727575}.
DISULFID 291 335 {ECO:0000269|PubMed:20727575}.
DISULFID 493 511 {ECO:0000269|PubMed:20727575}.
DISULFID 500 541 {ECO:0000269|PubMed:20727575}.
DISULFID 503 518 {ECO:0000269|PubMed:20727575}.
DISULFID 566 613 {ECO:0000269|PubMed:20727575}.
DISULFID 587 596 {ECO:0000269|PubMed:20727575}.
VAR_SEQ 111 124 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045349.
VARIANT 115 115 S -> T (in dbSNP:rs16968733).
{ECO:0000269|Ref.6}.
/FTId=VAR_029282.
VARIANT 207 207 R -> Q (rare polymorphism that results in
JMH-variant phenotype; dbSNP:rs55637216).
{ECO:0000269|PubMed:17207242}.
/FTId=VAR_038836.
VARIANT 207 207 R -> W (rare polymorphism that results in
JMH-variant phenotype; dbSNP:rs56367230).
{ECO:0000269|PubMed:17207242}.
/FTId=VAR_038837.
VARIANT 347 347 R -> L (rare polymorphism that results in
JMH-variant phenotype;
dbSNP:rs387907241).
{ECO:0000269|PubMed:20854351}.
/FTId=VAR_068679.
VARIANT 460 460 R -> H (rare polymorphism that results in
JMH-variant phenotype; dbSNP:rs56204206).
{ECO:0000269|PubMed:17207242}.
/FTId=VAR_038838.
VARIANT 461 461 R -> C (rare polymorphism that results in
JMH-variant phenotype; dbSNP:rs56001514).
{ECO:0000269|PubMed:17207242}.
/FTId=VAR_038839.
MUTAGEN 267 267 R->K: Abolishes ITGB1-dependent
enhancement of axon growth; when
associated with E-269.
{ECO:0000269|PubMed:12879062}.
MUTAGEN 269 269 D->E: Abolishes ITGB1-dependent
enhancement of axon growth; when
associated with K-267.
{ECO:0000269|PubMed:12879062}.
CONFLICT 545 545 K -> E (in Ref. 5; BAG56808).
{ECO:0000305}.
TURN 62 64 {ECO:0000244|PDB:3NVQ}.
STRAND 65 68 {ECO:0000244|PDB:3NVQ}.
STRAND 77 79 {ECO:0000244|PDB:3NVQ}.
STRAND 85 90 {ECO:0000244|PDB:3NVQ}.
STRAND 92 99 {ECO:0000244|PDB:3NVQ}.
STRAND 110 112 {ECO:0000244|PDB:3NVQ}.
STRAND 129 136 {ECO:0000244|PDB:3NVQ}.
STRAND 139 144 {ECO:0000244|PDB:3NVQ}.
TURN 146 148 {ECO:0000244|PDB:3NVQ}.
STRAND 151 158 {ECO:0000244|PDB:3NVQ}.
STRAND 160 165 {ECO:0000244|PDB:3NVQ}.
STRAND 180 183 {ECO:0000244|PDB:3NVQ}.
STRAND 186 189 {ECO:0000244|PDB:3NVQ}.
STRAND 204 210 {ECO:0000244|PDB:3NVQ}.
STRAND 223 230 {ECO:0000244|PDB:3NVQ}.
HELIX 235 237 {ECO:0000244|PDB:3NVQ}.
STRAND 239 247 {ECO:0000244|PDB:3NVQ}.
STRAND 257 266 {ECO:0000244|PDB:3NVQ}.
STRAND 272 274 {ECO:0000244|PDB:3NVQ}.
TURN 275 279 {ECO:0000244|PDB:3NVQ}.
STRAND 285 289 {ECO:0000244|PDB:3NVQ}.
TURN 294 296 {ECO:0000244|PDB:3NVQ}.
STRAND 302 309 {ECO:0000244|PDB:3NVQ}.
HELIX 316 318 {ECO:0000244|PDB:3NVQ}.
STRAND 320 326 {ECO:0000244|PDB:3NVQ}.
STRAND 332 338 {ECO:0000244|PDB:3NVQ}.
HELIX 339 348 {ECO:0000244|PDB:3NVQ}.
STRAND 368 370 {ECO:0000244|PDB:3NVQ}.
HELIX 375 383 {ECO:0000244|PDB:3NVQ}.
STRAND 386 389 {ECO:0000244|PDB:3NVQ}.
STRAND 394 397 {ECO:0000244|PDB:3NVQ}.
STRAND 401 406 {ECO:0000244|PDB:3NVQ}.
STRAND 408 417 {ECO:0000244|PDB:3NVQ}.
STRAND 423 431 {ECO:0000244|PDB:3NVQ}.
STRAND 436 440 {ECO:0000244|PDB:3NVQ}.
STRAND 451 456 {ECO:0000244|PDB:3NVQ}.
STRAND 467 471 {ECO:0000244|PDB:3NVQ}.
TURN 472 475 {ECO:0000244|PDB:3NVQ}.
STRAND 476 480 {ECO:0000244|PDB:3NVQ}.
STRAND 482 489 {ECO:0000244|PDB:3NVQ}.
HELIX 499 505 {ECO:0000244|PDB:3NVQ}.
STRAND 511 514 {ECO:0000244|PDB:3NVQ}.
STRAND 517 520 {ECO:0000244|PDB:3NVQ}.
STRAND 523 526 {ECO:0000244|PDB:3NVQ}.
STRAND 533 535 {ECO:0000244|PDB:3NVQ}.
TURN 537 540 {ECO:0000244|PDB:3NVQ}.
STRAND 541 545 {ECO:0000244|PDB:3NVQ}.
STRAND 551 556 {ECO:0000244|PDB:3NVQ}.
STRAND 562 567 {ECO:0000244|PDB:3NVQ}.
STRAND 573 579 {ECO:0000244|PDB:3NVQ}.
STRAND 582 587 {ECO:0000244|PDB:3NVQ}.
STRAND 592 602 {ECO:0000244|PDB:3NVQ}.
STRAND 609 619 {ECO:0000244|PDB:3NVQ}.
STRAND 621 631 {ECO:0000244|PDB:3NVQ}.
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


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