ID   CNTP2_HUMAN             Reviewed;        1331 AA.
AC   Q9UHC6; D3DWG2; Q14DG2; Q52LV1; Q5H9Q7; Q9UQ12;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 215.
DE   RecName: Full=Contactin-associated protein-like 2;
DE   AltName: Full=Cell recognition molecule Caspr2;
DE   Flags: Precursor;
GN   Name=CNTNAP2; Synonyms=CASPR2 {ECO:0000303|PubMed:10624965}, KIAA0868;
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 [MRNA] (ISOFORM 1), INTERACTION WITH KCNA2, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=10624965; DOI=10.1016/s0896-6273(00)81049-1;
RA   Poliak S., Gollan L., Martinez R., Custer A., Einheber S., Salzer J.L.,
RA   Trimmer J.S., Shrager P., Peles E.;
RT   "Caspr2, a new member of the neurexin superfamily, is localized at the
RT   juxtaparanodes of myelinated axons and associates with K+ channels.";
RL   Neuron 24:1037-1047(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=11352571; DOI=10.1006/geno.2001.6517;
RA   Nakabayashi K., Scherer S.W.;
RT   "The human contactin-associated protein-like 2 gene (CNTNAP2) spans over 2
RT   Mb of DNA at chromosome 7q35.";
RL   Genomics 73:108-112(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA   Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA   Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XII. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 5:355-364(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Retina;
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   [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
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   [7]
RP   INVOLVEMENT IN PTHSL1.
RX   PubMed=16571880; DOI=10.1056/nejmoa052773;
RA   Strauss K.A., Puffenberger E.G., Huentelman M.J., Gottlieb S., Dobrin S.E.,
RA   Parod J.M., Stephan D.A., Morton D.H.;
RT   "Recessive symptomatic focal epilepsy and mutant contactin-associated
RT   protein-like 2.";
RL   N. Engl. J. Med. 354:1370-1377(2006).
RN   [8]
RP   INVOLVEMENT IN PTHSL1.
RX   PubMed=19896112; DOI=10.1016/j.ajhg.2009.10.004;
RA   Zweier C., de Jong E.K., Zweier M., Orrico A., Ousager L.B., Collins A.L.,
RA   Bijlsma E.K., Oortveld M.A., Ekici A.B., Reis A., Schenck A., Rauch A.;
RT   "CNTNAP2 and NRXN1 are mutated in autosomal-recessive Pitt-Hopkins-like
RT   mental retardation and determine the level of a common synaptic protein in
RT   Drosophila.";
RL   Am. J. Hum. Genet. 85:655-666(2009).
RN   [9]
RP   FUNCTION.
RX   PubMed=33238150; DOI=10.1016/j.devcel.2020.10.020;
RA   Meng L., Yan D.;
RT   "NLR-1/CASPR Anchors F-Actin to Promote Gap Junction Formation.";
RL   Dev. Cell 55:574-587(2020).
RN   [10]
RP   INVOLVEMENT IN AUTS15, VARIANTS GLN-114; MET-218; MET-226; CYS-283;
RP   ASN-382; SER-407; ASP-418; LYS-680; GLN-699; CYS-716; SER-731; ASP-779;
RP   THR-869; HIS-906; ASN-1038; ALA-1102; GLY-1114; HIS-1119; HIS-1129;
RP   THR-1227; THR-1253 AND ILE-1278, AND CHROMOSOMAL REARRANGEMENT.
RX   PubMed=18179895; DOI=10.1016/j.ajhg.2007.09.017;
RA   Bakkaloglu B., O'Roak B.J., Louvi A., Gupta A.R., Abelson J.F.,
RA   Morgan T.M., Chawarska K., Klin A., Ercan-Sencicek A.G., Stillman A.A.,
RA   Tanriover G., Abrahams B.S., Duvall J.A., Robbins E.M., Geschwind D.H.,
RA   Biederer T., Gunel M., Lifton R.P., State M.W.;
RT   "Molecular cytogenetic analysis and resequencing of contactin associated
RT   protein-like 2 in autism spectrum disorders.";
RL   Am. J. Hum. Genet. 82:165-173(2008).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [12]
RP   INTERACTION WITH GPR37.
RX   PubMed=25977097; DOI=10.1111/jnc.13168;
RA   Tanabe Y., Fujita-Jimbo E., Momoi M.Y., Momoi T.;
RT   "CASPR2 forms a complex with GPR37 via MUPP1 but not with GPR37(R558Q), an
RT   autism spectrum disorder-related mutation.";
RL   J. Neurochem. 134:783-793(2015).
CC   -!- FUNCTION: Required for gap junction formation (Probable). Required,
CC       with CNTNAP1, for radial and longitudinal organization of myelinated
CC       axons. Plays a role in the formation of functional distinct domains
CC       critical for saltatory conduction of nerve impulses in myelinated nerve
CC       fibers. Demarcates the juxtaparanodal region of the axo-glial junction.
CC       {ECO:0000250|UniProtKB:Q9CPW0, ECO:0000305|PubMed:33238150}.
CC   -!- SUBUNIT: Interacts (via C-terminus) with KCNA2 (PubMed:10624965).
CC       Interacts with GPR37 (PubMed:25977097). {ECO:0000269|PubMed:10624965,
CC       ECO:0000269|PubMed:25977097}.
CC   -!- INTERACTION:
CC       Q9UHC6; Q12860: CNTN1; NbExp=5; IntAct=EBI-310892, EBI-5564336;
CC       Q9UHC6; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-310892, EBI-739467;
CC       Q9UHC6; P50222: MEOX2; NbExp=3; IntAct=EBI-310892, EBI-748397;
CC       Q9UHC6; P62487: POLR2G; NbExp=3; IntAct=EBI-310892, EBI-347928;
CC       Q9UHC6-1; P27824: CANX; NbExp=2; IntAct=EBI-16594440, EBI-355947;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9CPW0}; Single-
CC       pass type I membrane protein {ECO:0000305}. Cell projection, axon
CC       {ECO:0000250|UniProtKB:Q9CPW0}. Cell junction, paranodal septate
CC       junction {ECO:0000250|UniProtKB:Q9CPW0}. Note=Expressed in the
CC       juxtaparadonal region. {ECO:0000250|UniProtKB:Q9CPW0}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9UHC6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UHC6-2; Sequence=VSP_014976;
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in nervous system.
CC       {ECO:0000269|PubMed:10624965}.
CC   -!- DISEASE: Autism 15 (AUTS15) [MIM:612100]: A complex multifactorial,
CC       pervasive developmental disorder characterized by impairments in
CC       reciprocal social interaction and communication, restricted and
CC       stereotyped patterns of interests and activities, and the presence of
CC       developmental abnormalities by 3 years of age. Most individuals with
CC       autism also manifest moderate intellectual disability.
CC       {ECO:0000269|PubMed:18179895}. Note=Disease susceptibility is
CC       associated with variants affecting the gene represented in this entry.
CC   -!- DISEASE: Note=A chromosomal aberration involving CNTNAP2 is found in a
CC       patient with autism spectrum disorder. Paracentric inversion
CC       46,XY,inv(7)(q11.22;q35). The inversion breakpoints disrupt the genes
CC       AUTS2 and CNTNAP2.
CC   -!- DISEASE: Pitt-Hopkins-like syndrome 1 (PTHSL1) [MIM:610042]: A syndrome
CC       characterized by severe intellectual disability and variable additional
CC       symptoms, such as impaired speech development, seizures, autistic
CC       behavior, breathing anomalies and a broad mouth, resembling Pitt-
CC       Hopkins syndrome. In contrast to patients with Pitt-Hopkins syndrome,
CC       PTHSL1 patients present with normal or only mildly to moderately
CC       delayed motor milestones. {ECO:0000269|PubMed:16571880,
CC       ECO:0000269|PubMed:19896112}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA74891.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF193613; AAF25199.1; -; mRNA.
DR   EMBL; AF319045; AAK34932.1; -; mRNA.
DR   EMBL; AF318292; AAK49902.1; -; Genomic_DNA.
DR   EMBL; AF318298; AAK49903.1; -; Genomic_DNA.
DR   EMBL; AB020675; BAA74891.1; ALT_INIT; mRNA.
DR   EMBL; CR933671; CAI45967.1; -; mRNA.
DR   EMBL; CH471146; EAW80084.1; -; Genomic_DNA.
DR   EMBL; BC093780; AAH93780.1; -; mRNA.
DR   EMBL; BC113373; AAI13374.1; -; mRNA.
DR   CCDS; CCDS5889.1; -. [Q9UHC6-1]
DR   RefSeq; NP_054860.1; NM_014141.5. [Q9UHC6-1]
DR   PDB; 5Y4M; X-ray; 1.31 A; A=35-181.
DR   PDBsum; 5Y4M; -.
DR   AlphaFoldDB; Q9UHC6; -.
DR   SASBDB; Q9UHC6; -.
DR   SMR; Q9UHC6; -.
DR   BioGRID; 117510; 16.
DR   IntAct; Q9UHC6; 14.
DR   MINT; Q9UHC6; -.
DR   STRING; 9606.ENSP00000354778; -.
DR   GlyCosmos; Q9UHC6; 12 sites, No reported glycans.
DR   GlyGen; Q9UHC6; 12 sites.
DR   iPTMnet; Q9UHC6; -.
DR   PhosphoSitePlus; Q9UHC6; -.
DR   SwissPalm; Q9UHC6; -.
DR   BioMuta; CNTNAP2; -.
DR   DMDM; 17433089; -.
DR   EPD; Q9UHC6; -.
DR   jPOST; Q9UHC6; -.
DR   MassIVE; Q9UHC6; -.
DR   MaxQB; Q9UHC6; -.
DR   PaxDb; 9606-ENSP00000354778; -.
DR   PeptideAtlas; Q9UHC6; -.
DR   ProteomicsDB; 84311; -. [Q9UHC6-1]
DR   ProteomicsDB; 84312; -. [Q9UHC6-2]
DR   Pumba; Q9UHC6; -.
DR   ABCD; Q9UHC6; 1 sequenced antibody.
DR   Antibodypedia; 682; 341 antibodies from 32 providers.
DR   DNASU; 26047; -.
DR   Ensembl; ENST00000361727.8; ENSP00000354778.3; ENSG00000174469.23. [Q9UHC6-1]
DR   Ensembl; ENST00000463592.3; ENSP00000486292.1; ENSG00000174469.23. [Q9UHC6-2]
DR   Ensembl; ENST00000613345.2; ENSP00000481057.1; ENSG00000278728.2. [Q9UHC6-2]
DR   GeneID; 26047; -.
DR   KEGG; hsa:26047; -.
DR   MANE-Select; ENST00000361727.8; ENSP00000354778.3; NM_014141.6; NP_054860.1.
DR   UCSC; uc003weu.3; human. [Q9UHC6-1]
DR   AGR; HGNC:13830; -.
DR   CTD; 26047; -.
DR   DisGeNET; 26047; -.
DR   GeneCards; CNTNAP2; -.
DR   HGNC; HGNC:13830; CNTNAP2.
DR   HPA; ENSG00000174469; Group enriched (brain, retina).
DR   MalaCards; CNTNAP2; -.
DR   MIM; 604569; gene.
DR   MIM; 610042; phenotype.
DR   MIM; 612100; phenotype.
DR   neXtProt; NX_Q9UHC6; -.
DR   OpenTargets; ENSG00000174469; -.
DR   Orphanet; 163681; CNTNAP2-related developmental and epileptic encephalopathy.
DR   Orphanet; 106; NON RARE IN EUROPE: Autism.
DR   PharmGKB; PA26692; -.
DR   VEuPathDB; HostDB:ENSG00000174469; -.
DR   eggNOG; KOG3516; Eukaryota.
DR   GeneTree; ENSGT00940000154516; -.
DR   HOGENOM; CLU_003504_1_0_1; -.
DR   InParanoid; Q9UHC6; -.
DR   OMA; SRVQFNH; -.
DR   OrthoDB; 4255614at2759; -.
DR   PhylomeDB; Q9UHC6; -.
DR   TreeFam; TF321823; -.
DR   PathwayCommons; Q9UHC6; -.
DR   SignaLink; Q9UHC6; -.
DR   SIGNOR; Q9UHC6; -.
DR   BioGRID-ORCS; 26047; 11 hits in 1151 CRISPR screens.
DR   ChiTaRS; CNTNAP2; human.
DR   GeneWiki; CNTNAP2; -.
DR   GenomeRNAi; 26047; -.
DR   Pharos; Q9UHC6; Tbio.
DR   PRO; PR:Q9UHC6; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; Q9UHC6; Protein.
DR   Bgee; ENSG00000174469; Expressed in corpus callosum and 99 other cell types or tissues.
DR   ExpressionAtlas; Q9UHC6; baseline and differential.
DR   GO; GO:0030673; C:axolemma; IDA:BHF-UCL.
DR   GO; GO:0030424; C:axon; NAS:BHF-UCL.
DR   GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR   GO; GO:0030425; C:dendrite; NAS:BHF-UCL.
DR   GO; GO:0005769; C:early endosome; IDA:BHF-UCL.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:BHF-UCL.
DR   GO; GO:0044224; C:juxtaparanode region of axon; ISS:BHF-UCL.
DR   GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR   GO; GO:0043025; C:neuronal cell body; NAS:BHF-UCL.
DR   GO; GO:0033010; C:paranodal junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0033270; C:paranode region of axon; IEA:Ensembl.
DR   GO; GO:0043204; C:perikaryon; NAS:BHF-UCL.
DR   GO; GO:0097060; C:synaptic membrane; IEA:Ensembl.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:BHF-UCL.
DR   GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR   GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR   GO; GO:0044325; F:transmembrane transporter binding; IEA:Ensembl.
DR   GO; GO:0030534; P:adult behavior; IMP:BHF-UCL.
DR   GO; GO:0007420; P:brain development; TAS:BHF-UCL.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0008283; P:cell population proliferation; IDA:MGI.
DR   GO; GO:0021987; P:cerebral cortex development; IEP:BHF-UCL.
DR   GO; GO:0045163; P:clustering of voltage-gated potassium channels; ISS:BHF-UCL.
DR   GO; GO:0007612; P:learning; IMP:BHF-UCL.
DR   GO; GO:0021761; P:limbic system development; IEP:BHF-UCL.
DR   GO; GO:0031175; P:neuron projection development; ISS:BHF-UCL.
DR   GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
DR   GO; GO:0008038; P:neuron recognition; NAS:UniProtKB.
DR   GO; GO:1903598; P:positive regulation of gap junction assembly; IMP:UniProtKB.
DR   GO; GO:0060134; P:prepulse inhibition; IEA:Ensembl.
DR   GO; GO:0071205; P:protein localization to juxtaparanode region of axon; ISS:BHF-UCL.
DR   GO; GO:0035176; P:social behavior; IMP:BHF-UCL.
DR   GO; GO:0021756; P:striatum development; IEP:BHF-UCL.
DR   GO; GO:0071109; P:superior temporal gyrus development; IEP:BHF-UCL.
DR   GO; GO:0021794; P:thalamus development; IEP:BHF-UCL.
DR   GO; GO:0019226; P:transmission of nerve impulse; NAS:UniProtKB.
DR   GO; GO:0042297; P:vocal learning; IMP:BHF-UCL.
DR   GO; GO:0071625; P:vocalization behavior; IMP:BHF-UCL.
DR   CDD; cd00054; EGF_CA; 2.
DR   CDD; cd00057; FA58C; 1.
DR   CDD; cd00110; LamG; 4.
DR   Gene3D; 2.60.120.1000; -; 1.
DR   Gene3D; 2.60.120.200; -; 4.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.10.25.10; Laminin; 2.
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   NCBIfam; NF040941; GGGWT_bact; 1.
DR   PANTHER; PTHR15036:SF33; CONTACTIN-ASSOCIATED PROTEIN-LIKE 2; 1.
DR   PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 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; SSF49899; Concanavalin A-like lectins/glucanases; 4.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF56496; Fibrinogen C-terminal domain-like; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 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.
DR   Genevisible; Q9UHC6; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Autism; Autism spectrum disorder;
KW   Cell adhesion; Cell junction; Cell projection; Chromosomal rearrangement;
KW   Disulfide bond; EGF-like domain; Epilepsy; Glycoprotein;
KW   Intellectual disability; Membrane; Phosphoprotein; Reference proteome;
KW   Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..1331
FT                   /note="Contactin-associated protein-like 2"
FT                   /id="PRO_0000019506"
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..1331
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          216..368
FT                   /note="Laminin G-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          401..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          963..1002
FT                   /note="EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1055..1214
FT                   /note="Laminin G-like 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   REGION          1026..1045
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1303
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CPW0"
FT   MOD_RES         1306
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CPW0"
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        506
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        1116
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1198
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        1178..1214
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..1223
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_014976"
FT   VARIANT         114
FT                   /note="R -> Q (in dbSNP:rs189731792)"
FT                   /evidence="ECO:0000269|PubMed:18179895"
FT                   /id="VAR_046227"
FT   VARIANT         218
FT                   /note="T -> M (in dbSNP:rs771028883)"
FT                   /evidence="ECO:0000269|PubMed:18179895"
FT                   /id="VAR_046228"
FT   VARIANT         226
FT                   /note="L -> M (in dbSNP:rs372345438)"
FT                   /evidence="ECO:0000269|PubMed:18179895"
FT                   /id="VAR_046229"
FT   VARIANT         283
FT                   /note="R -> C (in dbSNP:rs794727802)"
FT                   /evidence="ECO:0000269|PubMed:18179895"
FT                   /id="VAR_046230"
FT   VARIANT         382
FT                   /note="S -> N (in dbSNP:rs371839994)"
FT                   /evidence="ECO:0000269|PubMed:18179895"
FT                   /id="VAR_046231"
FT   VARIANT         407
FT                   /note="N -> S (in dbSNP:rs143877693)"
FT                   /evidence="ECO:0000269|PubMed:18179895"
FT                   /id="VAR_046232"
FT   VARIANT         418
FT                   /note="N -> D (in dbSNP:rs772179690)"
FT                   /evidence="ECO:0000269|PubMed:18179895"
FT                   /id="VAR_046233"
FT   VARIANT         680
FT                   /note="E -> K (in dbSNP:rs368905425)"
FT                   /evidence="ECO:0000269|PubMed:18179895"
FT                   /id="VAR_046234"
FT   VARIANT         699
FT                   /note="P -> Q (in dbSNP:rs764412489)"
FT                   /evidence="ECO:0000269|PubMed:18179895"
FT                   /id="VAR_046235"
FT   VARIANT         716
FT                   /note="Y -> C (in dbSNP:rs760930032)"
FT                   /evidence="ECO:0000269|PubMed:18179895"
FT                   /id="VAR_046236"
FT   VARIANT         731
FT                   /note="G -> S (in dbSNP:rs369867547)"
FT                   /evidence="ECO:0000269|PubMed:18179895"
FT                   /id="VAR_046237"
FT   VARIANT         779
FT                   /note="G -> D (in dbSNP:rs200413148)"
FT                   /evidence="ECO:0000269|PubMed:18179895"
FT                   /id="VAR_046238"
FT   VARIANT         869
FT                   /note="I -> T (may be a risk factor for autism;
FT                   dbSNP:rs121908445)"
FT                   /evidence="ECO:0000269|PubMed:18179895"
FT                   /id="VAR_046239"
FT   VARIANT         906
FT                   /note="R -> H (in dbSNP:rs759801195)"
FT                   /evidence="ECO:0000269|PubMed:18179895"
FT                   /id="VAR_046240"
FT   VARIANT         1038
FT                   /note="D -> N (in dbSNP:rs144003410)"
FT                   /evidence="ECO:0000269|PubMed:18179895"
FT                   /id="VAR_046241"
FT   VARIANT         1102
FT                   /note="V -> A (in dbSNP:rs111599875)"
FT                   /evidence="ECO:0000269|PubMed:18179895"
FT                   /id="VAR_046242"
FT   VARIANT         1114
FT                   /note="S -> G (in dbSNP:rs983036503)"
FT                   /evidence="ECO:0000269|PubMed:18179895"
FT                   /id="VAR_046243"
FT   VARIANT         1119
FT                   /note="R -> H (in dbSNP:rs774709566)"
FT                   /evidence="ECO:0000269|PubMed:18179895"
FT                   /id="VAR_046244"
FT   VARIANT         1129
FT                   /note="D -> H (in dbSNP:rs781236853)"
FT                   /evidence="ECO:0000269|PubMed:18179895"
FT                   /id="VAR_046245"
FT   VARIANT         1227
FT                   /note="A -> T (in dbSNP:rs761684414)"
FT                   /evidence="ECO:0000269|PubMed:18179895"
FT                   /id="VAR_046246"
FT   VARIANT         1253
FT                   /note="I -> T (in dbSNP:rs767821521)"
FT                   /evidence="ECO:0000269|PubMed:18179895"
FT                   /id="VAR_046247"
FT   VARIANT         1278
FT                   /note="T -> I (in dbSNP:rs760047247)"
FT                   /evidence="ECO:0000269|PubMed:18179895"
FT                   /id="VAR_046248"
FT   STRAND          37..40
FT                   /evidence="ECO:0007829|PDB:5Y4M"
FT   HELIX           45..47
FT                   /evidence="ECO:0007829|PDB:5Y4M"
FT   STRAND          48..51
FT                   /evidence="ECO:0007829|PDB:5Y4M"
FT   HELIX           56..58
FT                   /evidence="ECO:0007829|PDB:5Y4M"
FT   HELIX           60..62
FT                   /evidence="ECO:0007829|PDB:5Y4M"
FT   STRAND          72..74
FT                   /evidence="ECO:0007829|PDB:5Y4M"
FT   STRAND          85..101
FT                   /evidence="ECO:0007829|PDB:5Y4M"
FT   STRAND          110..123
FT                   /evidence="ECO:0007829|PDB:5Y4M"
FT   STRAND          140..143
FT                   /evidence="ECO:0007829|PDB:5Y4M"
FT   STRAND          146..166
FT                   /evidence="ECO:0007829|PDB:5Y4M"
FT   STRAND          174..181
FT                   /evidence="ECO:0007829|PDB:5Y4M"
SQ   SEQUENCE   1331 AA;  148167 MW;  CFB2CB55BEFB99C2 CRC64;
     MQAAPRAGCG AALLLWIVSS CLCRAWTAPS TSQKCDEPLV SGLPHVAFSS SSSISGSYSP
     GYAKINKRGG AGGWSPSDSD HYQWLQVDFG NRKQISAIAT QGRYSSSDWV TQYRMLYSDT
     GRNWKPYHQD GNIWAFPGNI NSDGVVRHEL QHPIIARYVR IVPLDWNGEG RIGLRIEVYG
     CSYWADVINF DGHVVLPYRF RNKKMKTLKD VIALNFKTSE SEGVILHGEG QQGDYITLEL
     KKAKLVLSLN LGSNQLGPIY GHTSVMTGSL LDDHHWHSVV IERQGRSINL TLDRSMQHFR
     TNGEFDYLDL DYEITFGGIP FSGKPSSSSR KNFKGCMESI NYNGVNITDL ARRKKLEPSN
     VGNLSFSCVE PYTVPVFFNA TSYLEVPGRL NQDLFSVSFQ FRTWNPNGLL VFSHFADNLG
     NVEIDLTESK VGVHINITQT KMSQIDISSG SGLNDGQWHE VRFLAKENFA ILTIDGDEAS
     AVRTNSPLQV KTGEKYFFGG FLNQMNNSSH SVLQPSFQGC MQLIQVDDQL VNLYEVAQRK
     PGSFANVSID MCAIIDRCVP NHCEHGGKCS QTWDSFKCTC DETGYSGATC HNSIYEPSCE
     AYKHLGQTSN YYWIDPDGSG PLGPLKVYCN MTEDKVWTIV SHDLQMQTPV VGYNPEKYSV
     TQLVYSASMD QISAITDSAE YCEQYVSYFC KMSRLLNTPD GSPYTWWVGK ANEKHYYWGG
     SGPGIQKCAC GIERNCTDPK YYCNCDADYK QWRKDAGFLS YKDHLPVSQV VVGDTDRQGS
     EAKLSVGPLR CQGDRNYWNA ASFPNPSSYL HFSTFQGETS ADISFYFKTL TPWGVFLENM
     GKEDFIKLEL KSATEVSFSF DVGNGPVEIV VRSPTPLNDD QWHRVTAERN VKQASLQVDR
     LPQQIRKAPT EGHTRLELYS QLFVGGAGGQ QGFLGCIRSL RMNGVTLDLE ERAKVTSGFI
     SGCSGHCTSY GTNCENGGKC LERYHGYSCD CSNTAYDGTF CNKDVGAFFE EGMWLRYNFQ
     APATNARDSS SRVDNAPDQQ NSHPDLAQEE IRFSFSTTKA PCILLYISSF TTDFLAVLVK
     PTGSLQIRYN LGGTREPYNI DVDHRNMANG QPHSVNITRH EKTIFLKLDH YPSVSYHLPS
     SSDTLFNSPK SLFLGKVIET GKIDQEIHKY NTPGFTGCLS RVQFNQIAPL KAALRQTNAS
     AHVHIQGELV ESNCGASPLT LSPMSSATDP WHLDHLDSAS ADFPYNPGQG QAIRNGVNRN
     SAIIGGVIAV VIFTILCTLV FLIRYMFRHK GTYHTNEAKG AESAESADAA IMNNDPNFTE
     TIDESKKEWL I
//