PLXA4_HUMAN
ID PLXA4_HUMAN Reviewed; 1894 AA.
AC Q9HCM2; A4D1N6; E9PAM2; Q6UWC6; Q6ZW89; Q8N969; Q8ND00; Q8NEN3; Q9NTD4;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 4.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Plexin-A4;
DE Flags: Precursor;
GN Name=PLXNA4; Synonyms=KIAA1550, PLXNA4A, PLXNA4B;
GN ORFNames=UNQ2820/PRO34003;
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 [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
RC TISSUE=Brain, and Hippocampus;
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 [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., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., 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., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 194-1894 (ISOFORM 2).
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., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 206-1894 (ISOFORM 3), AND PARTIAL
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Kidney, and Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 433-1894 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [9]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1350, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
CC -!- FUNCTION: Coreceptor for SEMA3A. Necessary for signaling by class 3
CC semaphorins and subsequent remodeling of the cytoskeleton. Plays a role
CC in axon guidance in the developing nervous system. Class 3 semaphorins
CC bind to a complex composed of a neuropilin and a plexin. The plexin
CC modulates the affinity of the complex for specific semaphorins, and its
CC cytoplasmic domain is required for the activation of down-stream
CC signaling events in the cytoplasm (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with NRP1 and NRP2. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9HCM2-3; P42858: HTT; NbExp=3; IntAct=EBI-25962330, EBI-466029;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9HCM2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HCM2-2; Sequence=VSP_019331, VSP_019332;
CC Name=3;
CC IsoId=Q9HCM2-3; Sequence=VSP_019330, VSP_019333;
CC Name=4;
CC IsoId=Q9HCM2-4; Sequence=VSP_019334;
CC -!- SIMILARITY: Belongs to the plexin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ89209.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK095606; BAC04587.1; -; mRNA.
DR EMBL; AK123428; BAC85615.1; -; mRNA.
DR EMBL; AC009364; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC009365; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC009785; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011625; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC018643; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC026239; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236950; EAL24076.1; -; Genomic_DNA.
DR EMBL; CH471070; EAW83793.1; -; Genomic_DNA.
DR EMBL; BC028744; AAH28744.1; -; mRNA.
DR EMBL; AY358850; AAQ89209.1; ALT_INIT; mRNA.
DR EMBL; AL137352; CAB70707.1; -; mRNA.
DR EMBL; AL834504; CAD39161.3; -; mRNA.
DR EMBL; AB046770; BAB13376.3; -; mRNA.
DR CCDS; CCDS43646.1; -. [Q9HCM2-1]
DR CCDS; CCDS43647.1; -. [Q9HCM2-2]
DR CCDS; CCDS5826.1; -. [Q9HCM2-3]
DR PIR; T46426; T46426.
DR RefSeq; NP_001099013.1; NM_001105543.1. [Q9HCM2-2]
DR RefSeq; NP_065962.1; NM_020911.1. [Q9HCM2-1]
DR RefSeq; NP_861440.2; NM_181775.3. [Q9HCM2-3]
DR RefSeq; XP_005250743.1; XM_005250686.4. [Q9HCM2-1]
DR RefSeq; XP_006716234.1; XM_006716171.3. [Q9HCM2-1]
DR PDB; 4E74; X-ray; 1.58 A; A=1488-1603.
DR PDBsum; 4E74; -.
DR AlphaFoldDB; Q9HCM2; -.
DR SMR; Q9HCM2; -.
DR BioGRID; 124849; 33.
DR CORUM; Q9HCM2; -.
DR IntAct; Q9HCM2; 4.
DR STRING; 9606.ENSP00000352882; -.
DR GlyGen; Q9HCM2; 4 sites.
DR iPTMnet; Q9HCM2; -.
DR PhosphoSitePlus; Q9HCM2; -.
DR SwissPalm; Q9HCM2; -.
DR BioMuta; PLXNA4; -.
DR DMDM; 108860890; -.
DR EPD; Q9HCM2; -.
DR jPOST; Q9HCM2; -.
DR MassIVE; Q9HCM2; -.
DR MaxQB; Q9HCM2; -.
DR PaxDb; Q9HCM2; -.
DR PeptideAtlas; Q9HCM2; -.
DR PRIDE; Q9HCM2; -.
DR ProteomicsDB; 623; -.
DR ProteomicsDB; 81755; -. [Q9HCM2-1]
DR ProteomicsDB; 81756; -. [Q9HCM2-2]
DR ProteomicsDB; 81757; -. [Q9HCM2-3]
DR ProteomicsDB; 81758; -. [Q9HCM2-4]
DR Antibodypedia; 32143; 207 antibodies from 26 providers.
DR DNASU; 91584; -.
DR Ensembl; ENST00000321063.9; ENSP00000323194.4; ENSG00000221866.10. [Q9HCM2-1]
DR Ensembl; ENST00000359827.7; ENSP00000352882.3; ENSG00000221866.10. [Q9HCM2-1]
DR Ensembl; ENST00000378539.5; ENSP00000367800.5; ENSG00000221866.10. [Q9HCM2-3]
DR Ensembl; ENST00000423507.6; ENSP00000392772.2; ENSG00000221866.10. [Q9HCM2-2]
DR GeneID; 91584; -.
DR KEGG; hsa:91584; -.
DR MANE-Select; ENST00000321063.9; ENSP00000323194.4; NM_020911.2; NP_065962.1.
DR UCSC; uc003vra.4; human. [Q9HCM2-1]
DR CTD; 91584; -.
DR DisGeNET; 91584; -.
DR GeneCards; PLXNA4; -.
DR HGNC; HGNC:9102; PLXNA4.
DR HPA; ENSG00000221866; Tissue enhanced (adipose tissue, brain).
DR MIM; 604280; gene.
DR neXtProt; NX_Q9HCM2; -.
DR OpenTargets; ENSG00000221866; -.
DR PharmGKB; PA162399757; -.
DR VEuPathDB; HostDB:ENSG00000221866; -.
DR eggNOG; KOG3610; Eukaryota.
DR GeneTree; ENSGT01050000244850; -.
DR HOGENOM; CLU_001436_2_0_1; -.
DR InParanoid; Q9HCM2; -.
DR OMA; KVYLYKC; -.
DR OrthoDB; 503281at2759; -.
DR PhylomeDB; Q9HCM2; -.
DR TreeFam; TF312962; -.
DR PathwayCommons; Q9HCM2; -.
DR Reactome; R-HSA-399954; Sema3A PAK dependent Axon repulsion.
DR Reactome; R-HSA-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
DR Reactome; R-HSA-399956; CRMPs in Sema3A signaling.
DR Reactome; R-HSA-416700; Other semaphorin interactions.
DR Reactome; R-HSA-9615017; FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes.
DR SignaLink; Q9HCM2; -.
DR SIGNOR; Q9HCM2; -.
DR BioGRID-ORCS; 91584; 10 hits in 1073 CRISPR screens.
DR ChiTaRS; PLXNA4; human.
DR GeneWiki; PLXNA4A; -.
DR GenomeRNAi; 91584; -.
DR Pharos; Q9HCM2; Tbio.
DR PRO; PR:Q9HCM2; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9HCM2; protein.
DR Bgee; ENSG00000221866; Expressed in buccal mucosa cell and 161 other tissues.
DR ExpressionAtlas; Q9HCM2; baseline and differential.
DR Genevisible; Q9HCM2; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0002116; C:semaphorin receptor complex; IBA:GO_Central.
DR GO; GO:0017154; F:semaphorin receptor activity; IBA:GO_Central.
DR GO; GO:0021960; P:anterior commissure morphogenesis; IEA:Ensembl.
DR GO; GO:0021793; P:chemorepulsion of branchiomotor axon; IEA:Ensembl.
DR GO; GO:0035050; P:embryonic heart tube development; IEA:Ensembl.
DR GO; GO:0021612; P:facial nerve structural organization; IEA:Ensembl.
DR GO; GO:0021615; P:glossopharyngeal nerve morphogenesis; IEA:Ensembl.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IBA:GO_Central.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IBA:GO_Central.
DR GO; GO:0021784; P:postganglionic parasympathetic fiber development; IEA:Ensembl.
DR GO; GO:0048841; P:regulation of axon extension involved in axon guidance; IEA:Ensembl.
DR GO; GO:0030334; P:regulation of cell migration; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:0043087; P:regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0050923; P:regulation of negative chemotaxis; IEA:Ensembl.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; NAS:BHF-UCL.
DR GO; GO:1902287; P:semaphorin-plexin signaling pathway involved in axon guidance; IBA:GO_Central.
DR GO; GO:0048485; P:sympathetic nervous system development; IEA:Ensembl.
DR GO; GO:0097492; P:sympathetic neuron axon guidance; IEA:Ensembl.
DR GO; GO:0021637; P:trigeminal nerve structural organization; IEA:Ensembl.
DR GO; GO:0021644; P:vagus nerve morphogenesis; IEA:Ensembl.
DR Gene3D; 1.10.506.10; -; 1.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 2.60.40.10; -; 4.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR InterPro; IPR031148; Plexin.
DR InterPro; IPR013548; Plexin_cytoplasmic_RasGAP_dom.
DR InterPro; IPR002165; Plexin_repeat.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR001627; Semap_dom.
DR InterPro; IPR036352; Semap_dom_sf.
DR InterPro; IPR041019; TIG1_plexin.
DR InterPro; IPR041362; TIG2_plexin.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR22625; PTHR22625; 1.
DR Pfam; PF08337; Plexin_cytopl; 1.
DR Pfam; PF01437; PSI; 2.
DR Pfam; PF01403; Sema; 1.
DR Pfam; PF01833; TIG; 4.
DR Pfam; PF18020; TIG_2; 1.
DR Pfam; PF17960; TIG_plexin; 1.
DR SMART; SM00429; IPT; 4.
DR SMART; SM00423; PSI; 3.
DR SMART; SM00630; Sema; 1.
DR SUPFAM; SSF101912; SSF101912; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF81296; SSF81296; 4.
DR PROSITE; PS51004; SEMA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell membrane;
KW Disulfide bond; Glycoprotein; Membrane; Receptor; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1894
FT /note="Plexin-A4"
FT /id="PRO_0000240283"
FT TOPO_DOM 24..1237
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1238..1258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1259..1894
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 24..507
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 509..559
FT /note="PSI 1"
FT DOMAIN 655..702
FT /note="PSI 2"
FT DOMAIN 803..856
FT /note="PSI 3"
FT DOMAIN 858..952
FT /note="IPT/TIG 1"
FT DOMAIN 954..1037
FT /note="IPT/TIG 2"
FT DOMAIN 1040..1139
FT /note="IPT/TIG 3"
FT DOMAIN 1142..1230
FT /note="IPT/TIG 4"
FT MOD_RES 1350
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CARBOHYD 655
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1007
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 95..104
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 130..138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 284..405
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 300..356
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 374..393
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 510..527
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 516..558
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 519..536
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 530..542
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 593..612
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT VAR_SEQ 1..1550
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_019334"
FT VAR_SEQ 458..522
FT /note="IRVDGPRGNALQYETVQVVDPGPVLRDMAFSKDHEQLYIMSERQLTRVPVES
FT CGQYQSCGECLGS -> SFGTGPQGGITQEWIGVEGDPPGANIASQEQMLCVYLQCSSH
FT KAISDQRVQPLLCCFLNVPGNSS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_019330"
FT VAR_SEQ 458..492
FT /note="IRVDGPRGNALQYETVQVVDPGPVLRDMAFSKDHE -> MPGTSLCPTLELQ
FT TGPRSHRATVTLELLFSSCSSN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_019331"
FT VAR_SEQ 493..1894
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_019332"
FT VAR_SEQ 523..1894
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_019333"
FT CONFLICT 1750
FT /note="N -> D (in Ref. 7; CAD39161)"
FT /evidence="ECO:0000305"
FT CONFLICT 1804
FT /note="I -> V (in Ref. 7; CAD39161)"
FT /evidence="ECO:0000305"
FT STRAND 1499..1504
FT /evidence="ECO:0007829|PDB:4E74"
FT STRAND 1515..1520
FT /evidence="ECO:0007829|PDB:4E74"
FT HELIX 1525..1536
FT /evidence="ECO:0007829|PDB:4E74"
FT TURN 1537..1539
FT /evidence="ECO:0007829|PDB:4E74"
FT HELIX 1542..1544
FT /evidence="ECO:0007829|PDB:4E74"
FT HELIX 1548..1550
FT /evidence="ECO:0007829|PDB:4E74"
FT STRAND 1551..1556
FT /evidence="ECO:0007829|PDB:4E74"
FT STRAND 1562..1565
FT /evidence="ECO:0007829|PDB:4E74"
FT STRAND 1567..1569
FT /evidence="ECO:0007829|PDB:4E74"
FT HELIX 1584..1587
FT /evidence="ECO:0007829|PDB:4E74"
FT STRAND 1594..1599
FT /evidence="ECO:0007829|PDB:4E74"
FT CONFLICT Q9HCM2-2:458
FT /note="M -> V (in Ref. 1; BAC85615 and 6; AAQ89209)"
FT /evidence="ECO:0000305"
FT CONFLICT Q9HCM2-3:475
FT /note="E -> A (in Ref. 5; AAH28744)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1894 AA; 212455 MW; 7B45C8929C5847DF CRC64;
MKAMPWNWTC LLSHLLMVGM GSSTLLTRQP APLSQKQRSF VTFRGEPAEG FNHLVVDERT
GHIYLGAVNR IYKLSSDLKV LVTHETGPDE DNPKCYPPRI VQTCNEPLTT TNNVNKMLLI
DYKENRLIAC GSLYQGICKL LRLEDLFKLG EPYHKKEHYL SGVNESGSVF GVIVSYSNLD
DKLFIATAVD GKPEYFPTIS SRKLTKNSEA DGMFAYVFHD EFVASMIKIP SDTFTIIPDF
DIYYVYGFSS GNFVYFLTLQ PEMVSPPGST TKEQVYTSKL VRLCKEDTAF NSYVEVPIGC
ERSGVEYRLL QAAYLSKAGA VLGRTLGVHP DDDLLFTVFS KGQKRKMKSL DESALCIFIL
KQINDRIKER LQSCYRGEGT LDLAWLKVKD IPCSSALLTI DDNFCGLDMN APLGVSDMVR
GIPVFTEDRD RMTSVIAYVY KNHSLAFVGT KSGKLKKIRV DGPRGNALQY ETVQVVDPGP
VLRDMAFSKD HEQLYIMSER QLTRVPVESC GQYQSCGECL GSGDPHCGWC VLHNTCTRKE
RCERSKEPRR FASEMKQCVR LTVHPNNISV SQYNVLLVLE TYNVPELSAG VNCTFEDLSE
MDGLVVGNQI QCYSPAAKEV PRIITENGDH HVVQLQLKSK ETGMTFASTS FVFYNCSVHN
SCLSCVESPY RCHWCKYRHV CTHDPKTCSF QEGRVKLPED CPQLLRVDKI LVPVEVIKPI
TLKAKNLPQP QSGQRGYECI LNIQGSEQRV PALRFNSSSV QCQNTSYSYE GMEINNLPVE
LTVVWNGHFN IDNPAQNKVH LYKCGAMRES CGLCLKADPD FACGWCQGPG QCTLRQHCPA
QESQWLELSG AKSKCTNPRI TEIIPVTGPR EGGTKVTIRG ENLGLEFRDI ASHVKVAGVE
CSPLVDGYIP AEQIVCEMGE AKPSQHAGFV EICVAVCRPE FMARSSQLYY FMTLTLSDLK
PSRGPMSGGT QVTITGTNLN AGSNVVVMFG KQPCLFHRRS PSYIVCNTTS SDEVLEMKVS
VQVDRAKIHQ DLVFQYVEDP TIVRIEPEWS IVSGNTPIAV WGTHLDLIQN PQIRAKHGGK
EHINICEVLN ATEMTCQAPA LALGPDHQSD LTERPEEFGF ILDNVQSLLI LNKTNFTYYP
NPVFEAFGPS GILELKPGTP IILKGKNLIP PVAGGNVKLN YTVLVGEKPC TVTVSDVQLL
CESPNLIGRH KVMARVGGME YSPGMVYIAP DSPLSLPAIV SIAVAGGLLI IFIVAVLIAY
KRKSRESDLT LKRLQMQMDN LESRVALECK EAFAELQTDI HELTSDLDGA GIPFLDYRTY
TMRVLFPGIE DHPVLRDLEV PGYRQERVEK GLKLFAQLIN NKVFLLSFIR TLESQRSFSM
RDRGNVASLI MTVLQSKLEY ATDVLKQLLA DLIDKNLESK NHPKLLLRRT ESVAEKMLTN
WFTFLLYKFL KECAGEPLFS LFCAIKQQME KGPIDAITGE ARYSLSEDKL IRQQIDYKTL
VLSCVSPDNA NSPEVPVKIL NCDTITQVKE KILDAIFKNV PCSHRPKAAD MDLEWRQGSG
ARMILQDEDI TTKIENDWKR LNTLAHYQVP DGSVVALVSK QVTAYNAVNN STVSRTSASK
YENMIRYTGS PDSLRSRTPM ITPDLESGVK MWHLVKNHEH GDQKEGDRGS KMVSEIYLTR
LLATKGTLQK FVDDLFETIF STAHRGSALP LAIKYMFDFL DEQADKHGIH DPHVRHTWKS
NCLPLRFWVN MIKNPQFVFD IHKNSITDAC LSVVAQTFMD SCSTSEHRLG KDSPSNKLLY
AKDIPSYKNW VERYYSDIGK MPAISDQDMN AYLAEQSRMH MNEFNTMSAL SEIFSYVGKY
SEEILGPLDH DDQCGKQKLA YKLEQVITLM SLDS
