CNTP2_MOUSE
ID CNTP2_MOUSE Reviewed; 1332 AA.
AC Q9CPW0; Q6P2K4; Q6ZQ31;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Contactin-associated protein-like 2;
DE AltName: Full=Cell recognition molecule Caspr2;
DE Flags: Precursor;
GN Name=Cntnap2; Synonyms=Kiaa0868;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 295-1332 (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary gland;
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH KCNA2, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=11567047; DOI=10.1523/jneurosci.21-19-07568.2001;
RA Poliak S., Gollan L., Salomon D., Berglund E.O., Ohara R., Ranscht B.,
RA Peles E.;
RT "Localization of Caspr2 in myelinated nerves depends on axon-glia
RT interactions and the generation of barriers along the axon.";
RL J. Neurosci. 21:7568-7575(2001).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1304 AND SER-1307, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RX PubMed=25378149; DOI=10.1523/jneurosci.3369-14.2014;
RA Gordon A., Adamsky K., Vainshtein A., Frechter S., Dupree J.L.,
RA Rosenbluth J., Peles E.;
RT "Caspr and caspr2 are required for both radial and longitudinal
RT organization of myelinated axons.";
RL J. Neurosci. 34:14820-14826(2014).
CC -!- FUNCTION: Required for gap junction formation (By similarity).
CC Required, with CNTNAP1, for radial and longitudinal organization of
CC myelinated axons (PubMed:25378149). Plays a role in the formation of
CC functional distinct domains critical for saltatory conduction of nerve
CC impulses in myelinated nerve fibers. Demarcates the juxtaparanodal
CC region of the axo-glial junction (Probable) (PubMed:25378149).
CC {ECO:0000250|UniProtKB:Q9UHC6, ECO:0000269|PubMed:25378149,
CC ECO:0000305|PubMed:11567047}.
CC -!- SUBUNIT: Interacts (via C-terminus) with KCNA2.
CC {ECO:0000269|PubMed:11567047}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11567047}; Single-
CC pass type I membrane protein {ECO:0000305}. Cell projection, axon
CC {ECO:0000269|PubMed:11567047, ECO:0000269|PubMed:25378149}. Cell
CC junction, paranodal septate junction {ECO:0000269|PubMed:25378149}.
CC Note=Expressed in the juxtaparadonal region.
CC {ECO:0000269|PubMed:25378149}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9CPW0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CPW0-2; Sequence=VSP_014977;
CC -!- TISSUE SPECIFICITY: In sciatic nerve predominantly found at the
CC juxtaparanodal regions (at protein level).
CC {ECO:0000269|PubMed:11567047, ECO:0000269|PubMed:25378149}.
CC -!- DEVELOPMENTAL STAGE: Detected at postnatal day 8 in sciatic nerve at
CC the paranodes and the juxtaparanodal region. Is progressively
CC translocated to the adjacent juxtaparanodal region until it becomes
CC completely absent from the paranodes in the adult.
CC {ECO:0000269|PubMed:11567047}.
CC -!- DISRUPTION PHENOTYPE: Mutants don't show difference of Ranvier nodes
CC length and width compared to wild-type littermates. Double mutants
CC CNTNAP1 and CNTNAP2 have wider Ranvier nodes.
CC {ECO:0000269|PubMed:25378149}.
CC -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98042.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK017341; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK013139; BAB28674.1; -; mRNA.
DR EMBL; AK129232; BAC98042.1; ALT_INIT; mRNA.
DR EMBL; BC029826; AAH29826.1; -; mRNA.
DR EMBL; BC064467; AAH64467.1; -; mRNA.
DR CCDS; CCDS20094.1; -. [Q9CPW0-2]
DR CCDS; CCDS39475.1; -. [Q9CPW0-1]
DR RefSeq; NP_001004357.2; NM_001004357.2.
DR RefSeq; NP_080047.1; NM_025771.3. [Q9CPW0-2]
DR AlphaFoldDB; Q9CPW0; -.
DR SMR; Q9CPW0; -.
DR BioGRID; 211725; 23.
DR CORUM; Q9CPW0; -.
DR STRING; 10090.ENSMUSP00000110288; -.
DR GlyConnect; 2231; 16 N-Linked glycans (7 sites).
DR GlyGen; Q9CPW0; 11 sites, 16 N-linked glycans (7 sites).
DR iPTMnet; Q9CPW0; -.
DR PhosphoSitePlus; Q9CPW0; -.
DR SwissPalm; Q9CPW0; -.
DR MaxQB; Q9CPW0; -.
DR PaxDb; Q9CPW0; -.
DR PeptideAtlas; Q9CPW0; -.
DR PRIDE; Q9CPW0; -.
DR ProteomicsDB; 283665; -. [Q9CPW0-1]
DR ProteomicsDB; 283666; -. [Q9CPW0-2]
DR ABCD; Q9CPW0; 1 sequenced antibody.
DR Antibodypedia; 682; 294 antibodies from 32 providers.
DR DNASU; 66797; -.
DR Ensembl; ENSMUST00000060839; ENSMUSP00000056299; ENSMUSG00000039419. [Q9CPW0-2]
DR Ensembl; ENSMUST00000199100; ENSMUSP00000143528; ENSMUSG00000039419. [Q9CPW0-2]
DR GeneID; 66797; -.
DR KEGG; mmu:66797; -.
DR CTD; 26047; -.
DR MGI; MGI:1914047; Cntnap2.
DR VEuPathDB; HostDB:ENSMUSG00000039419; -.
DR eggNOG; KOG3516; Eukaryota.
DR GeneTree; ENSGT00940000154516; -.
DR InParanoid; Q9CPW0; -.
DR OrthoDB; 338397at2759; -.
DR PhylomeDB; Q9CPW0; -.
DR BioGRID-ORCS; 66797; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Cntnap2; mouse.
DR PRO; PR:Q9CPW0; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9CPW0; protein.
DR Bgee; ENSMUSG00000039419; Expressed in substantia nigra and 168 other tissues.
DR ExpressionAtlas; Q9CPW0; baseline and differential.
DR Genevisible; Q9CPW0; MM.
DR GO; GO:0030673; C:axolemma; ISS:BHF-UCL.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0043194; C:axon initial segment; IDA:MGI.
DR GO; GO:0009986; C:cell surface; ISS:BHF-UCL.
DR GO; GO:0150048; C:cerebellar granule cell to Purkinje cell synapse; IDA:MGI.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0005769; C:early endosome; ISS:BHF-UCL.
DR GO; GO:0060076; C:excitatory synapse; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISS:BHF-UCL.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0044224; C:juxtaparanode region of axon; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:BHF-UCL.
DR GO; GO:0043005; C:neuron projection; IMP:MGI.
DR GO; GO:0044309; C:neuron spine; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0033010; C:paranodal junction; IEA:UniProtKB-SubCell.
DR GO; GO:0044853; C:plasma membrane raft; IDA:MGI.
DR GO; GO:0098794; C:postsynapse; IDA:MGI.
DR GO; GO:0098793; C:presynapse; IDA:MGI.
DR GO; GO:0048787; C:presynaptic active zone membrane; IDA:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISS:BHF-UCL.
DR GO; GO:0030165; F:PDZ domain binding; IPI:MGI.
DR GO; GO:0099610; P:action potential initiation; IMP:MGI.
DR GO; GO:0030534; P:adult behavior; ISO:MGI.
DR GO; GO:0008306; P:associative learning; IMP:MGI.
DR GO; GO:0007409; P:axonogenesis; IMP:MGI.
DR GO; GO:0048266; P:behavioral response to pain; IGI:MGI.
DR GO; GO:0007155; P:cell adhesion; TAS:BHF-UCL.
DR GO; GO:0000902; P:cell morphogenesis; IMP:MGI.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0022010; P:central nervous system myelination; IMP:MGI.
DR GO; GO:0021692; P:cerebellar Purkinje cell layer morphogenesis; IMP:MGI.
DR GO; GO:0021549; P:cerebellum development; IMP:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI.
DR GO; GO:0042745; P:circadian sleep/wake cycle; IMP:MGI.
DR GO; GO:0045163; P:clustering of voltage-gated potassium channels; IMP:BHF-UCL.
DR GO; GO:0140059; P:dendrite arborization; IMP:MGI.
DR GO; GO:0060996; P:dendritic spine development; IMP:MGI.
DR GO; GO:0097062; P:dendritic spine maintenance; IMP:MGI.
DR GO; GO:0097061; P:dendritic spine organization; IMP:MGI.
DR GO; GO:1990403; P:embryonic brain development; IMP:MGI.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IMP:MGI.
DR GO; GO:0098976; P:excitatory chemical synaptic transmission; IMP:MGI.
DR GO; GO:0060079; P:excitatory postsynaptic potential; IMP:MGI.
DR GO; GO:1904861; P:excitatory synapse assembly; IMP:MGI.
DR GO; GO:0045444; P:fat cell differentiation; IMP:MGI.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0014009; P:glial cell proliferation; IMP:MGI.
DR GO; GO:1905962; P:glutamatergic neuron differentiation; IMP:MGI.
DR GO; GO:0007625; P:grooming behavior; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0006954; P:inflammatory response; IGI:MGI.
DR GO; GO:0098977; P:inhibitory chemical synaptic transmission; IMP:MGI.
DR GO; GO:1904862; P:inhibitory synapse assembly; IMP:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IMP:MGI.
DR GO; GO:0007612; P:learning; IMP:MGI.
DR GO; GO:0021761; P:limbic system development; IEP:BHF-UCL.
DR GO; GO:0045475; P:locomotor rhythm; IMP:MGI.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0099558; P:maintenance of synapse structure; IMP:MGI.
DR GO; GO:0007005; P:mitochondrion organization; IMP:MGI.
DR GO; GO:0061744; P:motor behavior; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0042552; P:myelination; IGI:MGI.
DR GO; GO:1904456; P:negative regulation of neuronal action potential; IMP:MGI.
DR GO; GO:0032229; P:negative regulation of synaptic transmission, GABAergic; IMP:MGI.
DR GO; GO:0061351; P:neural precursor cell proliferation; IMP:MGI.
DR GO; GO:0098529; P:neuromuscular junction development, skeletal muscle fiber; IMP:MGI.
DR GO; GO:0050905; P:neuromuscular process; IMP:MGI.
DR GO; GO:0050884; P:neuromuscular process controlling posture; IMP:MGI.
DR GO; GO:0031175; P:neuron projection development; IGI:MGI.
DR GO; GO:0048812; P:neuron projection morphogenesis; IMP:UniProtKB.
DR GO; GO:0008038; P:neuron recognition; TAS:BHF-UCL.
DR GO; GO:0019228; P:neuronal action potential; IMP:MGI.
DR GO; GO:1903598; P:positive regulation of gap junction assembly; ISO:MGI.
DR GO; GO:1904457; P:positive regulation of neuronal action potential; IMP:MGI.
DR GO; GO:0097106; P:postsynaptic density organization; IMP:MGI.
DR GO; GO:0043491; P:protein kinase B signaling; IMP:MGI.
DR GO; GO:0008104; P:protein localization; IMP:MGI.
DR GO; GO:0071205; P:protein localization to juxtaparanode region of axon; IMP:UniProtKB.
DR GO; GO:0002021; P:response to dietary excess; IMP:MGI.
DR GO; GO:0009408; P:response to heat; IMP:MGI.
DR GO; GO:0009725; P:response to hormone; IMP:MGI.
DR GO; GO:0097396; P:response to interleukin-17; IMP:MGI.
DR GO; GO:0009642; P:response to light intensity; IMP:MGI.
DR GO; GO:0009612; P:response to mechanical stimulus; IMP:MGI.
DR GO; GO:1901558; P:response to metformin; IMP:MGI.
DR GO; GO:1990834; P:response to odorant; IMP:MGI.
DR GO; GO:0010033; P:response to organic substance; IMP:MGI.
DR GO; GO:0048265; P:response to pain; IMP:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:MGI.
DR GO; GO:0007622; P:rhythmic behavior; IMP:MGI.
DR GO; GO:0035176; P:social behavior; IMP:MGI.
DR GO; GO:0031929; P:TOR signaling; IMP:MGI.
DR GO; GO:0019226; P:transmission of nerve impulse; IMP:MGI.
DR GO; GO:0042297; P:vocal learning; ISO:MGI.
DR GO; GO:0071625; P:vocalization behavior; IMP:MGI.
DR GO; GO:0090659; P:walking behavior; IMP:MGI.
DR CDD; cd00057; FA58C; 1.
DR CDD; cd00110; LamG; 4.
DR InterPro; IPR029831; Caspr2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR036056; Fibrinogen-like_C.
DR InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR003585; Neurexin-like.
DR PANTHER; PTHR15036:SF33; PTHR15036:SF33; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF02210; Laminin_G_2; 4.
DR SMART; SM00294; 4.1m; 1.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00231; FA58C; 1.
DR SMART; SM00282; LamG; 4.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF49899; SSF49899; 4.
DR SUPFAM; SSF56496; SSF56496; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01285; FA58C_1; 1.
DR PROSITE; PS01286; FA58C_2; 1.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell junction; Cell projection;
KW Disulfide bond; EGF-like domain; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..1332
FT /note="Contactin-associated protein-like 2"
FT /id="PRO_0000019507"
FT TOPO_DOM 28..1262
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1263..1283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1284..1332
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..181
FT /note="F5/8 type C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DOMAIN 187..368
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 373..552
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 554..591
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 592..798
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DOMAIN 799..963
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 964..1002
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1023..1214
FT /note="Laminin G-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT MOD_RES 1304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1307
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 436
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 507
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 630
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 735
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 35..181
FT /evidence="ECO:0000250"
FT DISULFID 336..368
FT /evidence="ECO:0000250"
FT DISULFID 520..552
FT /evidence="ECO:0000250"
FT DISULFID 558..569
FT /evidence="ECO:0000250"
FT DISULFID 563..578
FT /evidence="ECO:0000250"
FT DISULFID 580..590
FT /evidence="ECO:0000250"
FT DISULFID 936..963
FT /evidence="ECO:0000250"
FT DISULFID 967..980
FT /evidence="ECO:0000250"
FT DISULFID 974..989
FT /evidence="ECO:0000250"
FT DISULFID 991..1001
FT /evidence="ECO:0000250"
FT DISULFID 1179..1215
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..1224
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_014977"
FT CONFLICT 357
FT /note="G -> E (in Ref. 3; AAH64467)"
FT /evidence="ECO:0000305"
FT CONFLICT 538
FT /note="Q -> H (in Ref. 3; AAH64467)"
FT /evidence="ECO:0000305"
FT CONFLICT 1192
FT /note="K -> N (in Ref. 3; AAH64467)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1332 AA; 148197 MW; 6AA097C69D83F0A5 CRC64;
MVMSLRAGYR AALSLWILSS FICRAWTAPS TFQKCDEPLI SGLPHVSFSS SSSLSSSYAP
GYAKINKRGG AGGWSPSDSD HYQWLQVDFG NRKQISAIAT QGRYSSSDWV TQYRMLYSDT
GRNWKPYHQD GNIWAFPGNI NSDSVVRHDL QHAVVARYVR IVPLDWNGEG HIGLRAEVYG
CAYWADVINF DGHGVLPYRF RNKKMKTLKD VIALKFKTSE SEGVLLHGEG QQGDYITLEL
KKAKLVLSLN LGSNQLGPIY GHTSVTSGSL LDDHHWHSVL IERQGRSINL TLDRSMQHFR
TNGEFDYLDL DYEITFGGIP FSGKPSSSNR KNFKGCMESI NYNGVNITDL ARRKKLGPSN
MGNLSFSCVE PYTVPVFFNA TSYLEVPGRL NQDLFSVSFQ FRTWNPSGLL LFSHFADNLG
NVEIDLVESK VGVHINNTQT KTSQIDISSG SGLNDGQWHE VRFLAKENFA VLTIDGDEAS
AVRTNSPLQV KTGEKYFFGG FLNHMNNASY SALQPSFQGC MQLIQVDDQL VNLYEVAQRK
PGSFANVTID MCAIIDRCVP NHCEHGGKCS QTWDSFKCTC DETGYSGATC HNSIYEPSCE
AYKHLGQTSN YYWIDPDGSG PLGPLKVYCN MTEDKVWTIV SHDLQMQTTV VGYNPEKYSV
TQLIYSASMD QISAITSSAE YCEQYVSYFC RMSRLLNTPD GSPYTWWVGK ANEKHYYWGG
SEPGIQKCAC GIERNCTDPK YYCNCDADYK QWRKDAGFLS YKDHLPVSQV VVGDTDRQGS
EAKLSVGPLR CQGDRNYWNA ASFPNPSSYL HFSTFQGETS ADISFYFKTL IPRGVFLENL
GNTDFIKLEL KSATEVSFSF DVGNGPVEIV VRSPSPLNDD QWHRVTAERN VKQASLQVDR
LPQQIRKAPT EGHTRLELYS QLFVGGAGGQ QGFLGCIRSL RMNGVTLDLE ERAKVTSGFK
SGCSGHCTSY GANCENGGKC IEKYHGYSCD CSNTAYDGTF CNKDVGAFFE EGMWLRYNFQ
APAVTARDTG SRAENSADQQ QHLAPDLAQE QIHFSFSTTK APCILLYVSS LTTDFLAVLV
KPTGNLQIRY NLGGTREPFN IDVDHRNMAN GQPHSVNITR HERTIILKLD HYPAVGYHLP
SSSDTLFNSP KSLFLGKVIE TGKIDQEIHK YNTPGFTGCL SRVQFNHIAP LKAALRQTNA
SAHVHIQGEL VESNCGASPL TLSPMSSATD PWHLDHLDSA SADFPYNPGQ GQAIRNGVNR
NSAIIGGVIA VVIFTILCTL VFLIRYMFRH KGTYHTNEAK GAESAESADA AIMNNDPNFT
ETIDESKKEW LI
