ID   COGA1_HUMAN             Reviewed;        1604 AA.
AC   Q07092; Q16593; Q59F89; Q71RG9;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   09-APR-2025, entry version 210.
DE   RecName: Full=Collagen alpha-1(XVI) chain;
DE   Flags: Precursor;
GN   Name=COL16A1; ORFNames=FP1572;
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), AND VARIANT LYS-62.
RC   TISSUE=Fibroblast;
RX   PubMed=1631157; DOI=10.1073/pnas.89.14.6565;
RA   Pan T.-C., Zhang R.-Z., Mattei M.-G., Timpl R., Chu M.-L.;
RT   "Cloning and chromosomal location of human alpha 1(XVI) collagen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:6565-6569(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [3]
RP   PROTEIN SEQUENCE OF 22-33, SUBUNIT, AND GLYCOSYLATION.
RX   PubMed=7882999; DOI=10.1111/j.1432-1033.1995.tb20245.x;
RA   Tillet E., Mann K., Nischt R., Pan T.-C., Chu M.-L., Timpl R.;
RT   "Recombinant analysis of human alpha 1 (XVI) collagen. Evidence for
RT   processing of the N-terminal globular domain.";
RL   Eur. J. Biochem. 228:160-168(1995).
RN   [4]
RP   PROTEIN SEQUENCE OF 22-30; 257-265 AND 941-950, SUBUNIT, INTERACTION WITH
RP   FBN1 AND FN1, AND GLYCOSYLATION.
RX   PubMed=15165854; DOI=10.1016/j.jmb.2004.03.042;
RA   Kassner A., Tiedemann K., Notbohm H., Ludwig T., Morgelin M.,
RA   Reinhardt D.P., Chu M.-L., Bruckner P., Grassel S.;
RT   "Molecular structure and interaction of recombinant human type XVI
RT   collagen.";
RL   J. Mol. Biol. 339:835-853(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 111-1604 (ISOFORM 2).
RC   TISSUE=Spleen;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 403-849.
RC   TISSUE=Placenta;
RA   Kimura S.;
RL   Submitted (APR-1989) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 418-1604 (ISOFORM 1).
RC   TISSUE=Placenta;
RX   PubMed=1284248; DOI=10.1093/oxfordjournals.jbchem.a123989;
RA   Yamaguchi N., Kimura S., McBride O.W., Hori H., Yamada Y., Kanamori T.,
RA   Yamakoshi H., Nagai Y.;
RT   "Molecular cloning and partial characterization of a novel collagen chain,
RT   alpha 1(XVI), consisting of repetitive collagenous domains and cysteine-
RT   containing non-collagenous segments.";
RL   J. Biochem. 112:856-863(1992).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1387-1604.
RX   PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA   Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA   Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA   Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT   "Large-scale cDNA transfection screening for genes related to cancer
RT   development and progression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN   [9]
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=9022684; DOI=10.1111/j.1432-1033.1996.0576r.x;
RA   Grassel S., Timpl R., Tan E.M.L., Chu M.-L.;
RT   "Biosynthesis and processing of type XVI collagen in human fibroblasts and
RT   smooth muscle cells.";
RL   Eur. J. Biochem. 242:576-584(1996).
RN   [10]
RP   TISSUE SPECIFICITY.
RX   PubMed=12782140; DOI=10.1016/s0945-053x(03)00008-8;
RA   Kassner A., Hansen U., Miosge N., Reinhardt D.P., Aigner T.,
RA   Bruckner-Tuderman L., Bruckner P., Grassel S.;
RT   "Discrete integration of collagen XVI into tissue-specific collagen fibrils
RT   or beaded microfibrils.";
RL   Matrix Biol. 22:131-143(2003).
RN   [11]
RP   FUNCTION, SUBUNIT, AND INTERACTION WITH INTEGRIN ALPHA-1/BETA-1 AND
RP   INTEGRIN ALPHA-2/BETA-1.
RX   PubMed=16754661; DOI=10.1074/jbc.m509942200;
RA   Eble J.A., Kassner A., Niland S., Morgelin M., Grifka J., Grassel S.;
RT   "Collagen XVI harbors an integrin alpha1 beta1 recognition site in its C-
RT   terminal domains.";
RL   J. Biol. Chem. 281:25745-25756(2006).
CC   -!- FUNCTION: Involved in mediating cell attachment and inducing integrin-
CC       mediated cellular reactions, such as cell spreading and alterations in
CC       cell morphology. {ECO:0000269|PubMed:16754661}.
CC   -!- SUBUNIT: Homotrimer. Interacts with FBN1, fibronectin and integrins
CC       ITGA1/ITGB1 and ITGA2/ITGB1. Integrin ITGA1/ITGB1 binds to a unique
CC       site within COL16A1 located close to its C-terminal end between
CC       collagenous domains COL1-COL3. {ECO:0000269|PubMed:15165854,
CC       ECO:0000269|PubMed:16754661, ECO:0000269|PubMed:7882999,
CC       ECO:0000269|PubMed:9022684}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000269|PubMed:9022684}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q07092-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q07092-2; Sequence=VSP_024259, VSP_024260;
CC   -!- TISSUE SPECIFICITY: In papillary dermis, is a component of specialized
CC       fibrillin-1-containing microfibrils, whereas in territorial cartilage
CC       matrix, it is localized to a discrete population of thin, weakly banded
CC       collagen fibrils in association with other collagens (at protein
CC       level). In the placenta, where it is found in the amnion, a membranous
CC       tissue lining the amniotic cavity. Within the amnion, it is found in an
CC       acellular, relatively dense layer of a complex network of reticular
CC       fibers. Also located to a fibroblast layer beneath this dense layer.
CC       Exists in tissues in association with other types of collagen.
CC       {ECO:0000269|PubMed:12782140}.
CC   -!- DEVELOPMENTAL STAGE: Transiently elevated expression during gestation,
CC       and decrease at term.
CC   -!- DOMAIN: This sequence defines eighteen different domains, nine triple-
CC       helical domains (COL9 to COL1) and ten non-triple-helical domains (NC10
CC       to NC1). The numerous interruptions in the triple helix may make this
CC       molecule either elastic or flexible.
CC   -!- PTM: Prolines at the third position of the tripeptide repeating unit
CC       (G-X-Y) are hydroxylated in some or all of the chains.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:15165854,
CC       ECO:0000269|PubMed:7882999}.
CC   -!- SIMILARITY: Belongs to the fibril-associated collagens with interrupted
CC       helices (FACIT) family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/44542/COL16A1";
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DR   EMBL; M92642; AAA58427.1; -; mRNA.
DR   EMBL; AC114488; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AB209571; BAD92808.1; -; mRNA.
DR   EMBL; X14963; CAA33085.1; -; mRNA.
DR   EMBL; X15038; CAA33142.1; -; mRNA.
DR   EMBL; S57132; AAB25797.1; -; mRNA.
DR   EMBL; AF370368; AAQ15204.1; -; mRNA.
DR   CCDS; CCDS41297.1; -. [Q07092-1]
DR   PIR; S23810; S23810.
DR   RefSeq; NP_001847.3; NM_001856.3. [Q07092-1]
DR   AlphaFoldDB; Q07092; -.
DR   BioGRID; 107703; 22.
DR   ComplexPortal; CPX-1757; Collagen type XVI trimer.
DR   IntAct; Q07092; 13.
DR   MINT; Q07092; -.
DR   STRING; 9606.ENSP00000362776; -.
DR   GlyConnect; 1133; 1 N-Linked glycan (1 site).
DR   GlyCosmos; Q07092; 2 sites, 1 glycan.
DR   GlyGen; Q07092; 2 sites, 1 N-linked glycan (1 site).
DR   iPTMnet; Q07092; -.
DR   PhosphoSitePlus; Q07092; -.
DR   BioMuta; COL16A1; -.
DR   DMDM; 143811380; -.
DR   jPOST; Q07092; -.
DR   MassIVE; Q07092; -.
DR   PaxDb; 9606-ENSP00000362776; -.
DR   PeptideAtlas; Q07092; -.
DR   ProteomicsDB; 58503; -. [Q07092-1]
DR   ProteomicsDB; 58504; -. [Q07092-2]
DR   Antibodypedia; 8436; 74 antibodies from 19 providers.
DR   DNASU; 1307; -.
DR   Ensembl; ENST00000373672.8; ENSP00000362776.3; ENSG00000084636.18. [Q07092-1]
DR   GeneID; 1307; -.
DR   KEGG; hsa:1307; -.
DR   MANE-Select; ENST00000373672.8; ENSP00000362776.3; NM_001856.4; NP_001847.3.
DR   UCSC; uc001btk.2; human. [Q07092-1]
DR   AGR; HGNC:2193; -.
DR   CTD; 1307; -.
DR   DisGeNET; 1307; -.
DR   GeneCards; COL16A1; -.
DR   HGNC; HGNC:2193; COL16A1.
DR   HPA; ENSG00000084636; Tissue enhanced (ovary).
DR   MIM; 120326; gene.
DR   neXtProt; NX_Q07092; -.
DR   OpenTargets; ENSG00000084636; -.
DR   PharmGKB; PA26709; -.
DR   VEuPathDB; HostDB:ENSG00000084636; -.
DR   eggNOG; KOG3544; Eukaryota.
DR   GeneTree; ENSGT00940000161782; -.
DR   HOGENOM; CLU_001074_2_2_1; -.
DR   InParanoid; Q07092; -.
DR   OMA; MGNSWQP; -.
DR   OrthoDB; 5983381at2759; -.
DR   PhylomeDB; Q07092; -.
DR   TreeFam; TF332900; -.
DR   PathwayCommons; Q07092; -.
DR   Reactome; R-HSA-1442490; Collagen degradation.
DR   Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
DR   Reactome; R-HSA-216083; Integrin cell surface interactions.
DR   Reactome; R-HSA-8948216; Collagen chain trimerization.
DR   SignaLink; Q07092; -.
DR   BioGRID-ORCS; 1307; 7 hits in 1139 CRISPR screens.
DR   ChiTaRS; COL16A1; human.
DR   GeneWiki; Collagen,_type_XVI,_alpha_1; -.
DR   GenomeRNAi; 1307; -.
DR   Pharos; Q07092; Tbio.
DR   PRO; PR:Q07092; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q07092; protein.
DR   Bgee; ENSG00000084636; Expressed in tibia and 198 other cell types or tissues.
DR   ExpressionAtlas; Q07092; baseline and differential.
DR   GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR   GO; GO:0005594; C:collagen type IX trimer; IBA:GO_Central.
DR   GO; GO:0005597; C:collagen type XVI trimer; TAS:ProtInc.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; HDA:BHF-UCL.
DR   GO; GO:0005178; F:integrin binding; IDA:UniProtKB.
DR   GO; GO:0007155; P:cell adhesion; IDA:UniProtKB.
DR   GO; GO:0033627; P:cell adhesion mediated by integrin; IDA:CACAO.
DR   GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
DR   GO; GO:0007565; P:female pregnancy; TAS:ProtInc.
DR   GO; GO:0033622; P:integrin activation; IDA:CACAO.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; TAS:UniProtKB.
DR   GO; GO:0051894; P:positive regulation of focal adhesion assembly; IDA:CACAO.
DR   FunFam; 2.60.120.200:FF:000094; Collagen type XVI alpha 1 chain; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR050149; Collagen_superfamily.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR048287; TSPN-like_N.
DR   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24023:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 1.
DR   Pfam; PF01391; Collagen; 9.
DR   SMART; SM00210; TSPN; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Collagen; Direct protein sequencing;
KW   Extracellular matrix; Glycoprotein; Hydroxylation;
KW   Proteomics identification; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:15165854,
FT                   ECO:0000269|PubMed:7882999"
FT   CHAIN           22..1604
FT                   /note="Collagen alpha-1(XVI) chain"
FT                   /id="PRO_0000005792"
FT   DOMAIN          50..231
FT                   /note="Laminin G-like"
FT   DOMAIN          375..423
FT                   /note="Collagen-like 1"
FT   DOMAIN          573..633
FT                   /note="Collagen-like 2"
FT   DOMAIN          667..721
FT                   /note="Collagen-like 3"
FT   DOMAIN          788..840
FT                   /note="Collagen-like 4"
FT   DOMAIN          888..938
FT                   /note="Collagen-like 5"
FT   DOMAIN          1018..1075
FT                   /note="Collagen-like 6"
FT   DOMAIN          1472..1524
FT                   /note="Collagen-like 7"
FT   DOMAIN          1528..1576
FT                   /note="Collagen-like 8"
FT   REGION          232..374
FT                   /note="Nonhelical region 10 (NC10)"
FT   REGION          301..509
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          375..506
FT                   /note="Triple-helical region 9 (COL9) with 3 imperfections"
FT   REGION          507..521
FT                   /note="Nonhelical region 9 (NC9)"
FT   REGION          522..555
FT                   /note="Triple-helical region 8 (COL8) with 1 imperfection"
FT   REGION          556..572
FT                   /note="Nonhelical region 8 (NC8)"
FT   REGION          573..631
FT                   /note="Triple-helical region 7 (COL7) with 1 imperfection"
FT   REGION          604..917
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          632..652
FT                   /note="Nonhelical region 7 (NC7)"
FT   REGION          653..723
FT                   /note="Triple-helical region 6 (COL6) with 1 imperfection"
FT   REGION          724..738
FT                   /note="Nonhelical region 6 (NC6)"
FT   REGION          739..876
FT                   /note="Triple-helical region 5 (COL5) with 3 imperfections"
FT   REGION          877..887
FT                   /note="Nonhelical region 5 (NC5)"
FT   REGION          888..939
FT                   /note="Triple-helical region 4 (COL4) with 2 imperfections"
FT   REGION          940..973
FT                   /note="Nonhelical region 4 (NC4)"
FT   REGION          974..988
FT                   /note="Triple-helical region 3 (COL3)"
FT   REGION          989..1011
FT                   /note="Nonhelical region 3 (NC3)"
FT   REGION          1001..1429
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1012..1433
FT                   /note="Triple-helical region 2 (COL2) with 2 imperfections"
FT   REGION          1434..1472
FT                   /note="Nonhelical region 2 (NC2)"
FT   REGION          1468..1517
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1473..1578
FT                   /note="Triple-helical region 1 (COL1) with 2 imperfections"
FT   REGION          1579..1604
FT                   /note="Nonhelical region 1 (NC1)"
FT   MOTIF           540..542
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   MOTIF           1006..1008
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   MOTIF           1227..1229
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        301..311
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        383..397
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..407
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        449..460
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        486..495
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        674..684
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        686..702
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        766..781
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        792..808
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        826..846
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        864..873
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        905..917
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1044..1055
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1160..1169
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1199..1208
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1217..1226
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1271..1284
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1286..1302
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1330..1342
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1369..1378
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1386..1395
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1420..1429
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        47
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        327
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1052
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.5"
FT                   /id="VSP_024259"
FT   VAR_SEQ         1161
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.5"
FT                   /id="VSP_024260"
FT   VARIANT         62
FT                   /note="T -> K (in dbSNP:rs2228552)"
FT                   /evidence="ECO:0000269|PubMed:1631157"
FT                   /id="VAR_031440"
FT   VARIANT         418
FT                   /note="R -> Q (in dbSNP:rs6699645)"
FT                   /id="VAR_048778"
FT   VARIANT         745
FT                   /note="G -> S (in dbSNP:rs34770879)"
FT                   /id="VAR_048779"
FT   CONFLICT        419
FT                   /note="D -> G (in Ref. 7; AAB25797)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        420..421
FT                   /note="GR -> A (in Ref. 1; AAA58427)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        538
FT                   /note="P -> R (in Ref. 1; AAA58427)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        848..849
FT                   /note="RD -> VM (in Ref. 6; CAA33142/CAA33085)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1161
FT                   /note="P -> T (in Ref. 1; AAA58427)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1164
FT                   /note="P -> T (in Ref. 1; AAA58427)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1166
FT                   /note="P -> S (in Ref. 1; AAA58427)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1604 AA;  157751 MW;  5FAA1950DFC6CA3C CRC64;
     MWVSWAPGLW LLGLWATFGH GANTGAQCPP SQQEGLKLEH SSSLPANVTG FNLIHRLSLM
     KTSAIKKIRN PKGPLILRLG AAPVTQPTRR VFPRGLPEEF ALVLTLLLKK HTHQKTWYLF
     QVTDANGYPQ ISLEVNSQER SLELRAQGQD GDFVSCIFPV PQLFDLRWHK LMLSVAGRVA
     SVHVDCSSAS SQPLGPRRPM RPVGHVFLGL DAEQGKPVSF DLQQVHIYCD PELVLEEGCC
     EILPAGCPPE TSKARRDTQS NELIEINPQS EGKVYTRCFC LEEPQNSEVD AQLTGRISQK
     AERGAKVHQE TAADECPPCV HGARDSNVTL APSGPKGGKG ERGLPGPPGS KGEKGARGND
     CVRISPDAPL QCAEGPKGEK GESGALGPSG LPGSTGEKGQ KGEKGDGGIK GVPGKPGRDG
     RPGEICVIGP KGQKGDPGFV GPEGLAGEPG PPGLPGPPGI GLPGTPGDPG GPPGPKGDKG
     SSGIPGKEGP GGKPGKPGVK GEKGDPCEVC PTLPEGFQNF VGLPGKPGPK GEPGDPVPAR
     GDPGIQGIKG EKGEPCLSCS SVVGAQHLVS STGASGDVGS PGFGLPGLPG RAGVPGLKGE
     KGNFGEAGPA GSPGPPGPVG PAGIKGAKGE PCEPCPALSN LQDGDVRVVA LPGPSGEKGE
     PGPPGFGLPG KQGKAGERGL KGQKGDAGNP GDPGTPGTTG RPGLSGEPGV QGPAGPKGEK
     GDGCTACPSL QGTVTDMAGR PGQPGPKGEQ GPEGVGRPGK PGQPGLPGVQ GPPGLKGVQG
     EPGPPGRGVQ GPQGEPGAPG LPGIQGLPGP RGPPGPTGEK GAQGSPGVKG ATGPVGPPGA
     SVSGPPGRDG QQGQTGLRGT PGEKGPRGEK GEPGECSCPS QGDLIFSGMP GAPGLWMGSS
     WQPGPQGPPG IPGPPGPPGV PGLQGVPGNN GLPGQPGLTA ELGSLPIEQH LLKSICGDCV
     QGQRAHPGYL VEKGEKGDQG IPGVPGLDNC AQCFLSLERP RAEEARGDNS EGDPGCVGSP
     GLPGPPGLPG QRGEEGPPGM RGSPGPPGPI GPPGFPGAVG SPGLPGLQGE RGLTGLTGDK
     GEPGPPGQPG YPGATGPPGL PGIKGERGYT GSAGEKGEPG PPGSEGLPGP PGPAGPRGER
     GPQGNSGEKG DQGFQGQPGF PGPPGPPGFP GKVGSPGPPG PQAEKGSEGI RGPSGLPGSP
     GPPGPPGIQG PAGLDGLDGK DGKPGLRGDP GPAGPPGLMG PPGFKGKTGH PGLPGPKGDC
     GKPGPPGSTG RPGAEGEPGA MGPQGRPGPP GHVGPPGPPG QPGPAGISAV GLKGDRGATG
     ERGLAGLPGQ PGPPGHPGPP GEPGTDGAAG KEGPPGKQGF YGPPGPKGDP GAAGQKGQAG
     EKGRAGMPGG PGKSGSMGPV GPPGPAGERG HPGAPGPSGS PGLPGVPGSM GDMVNYDEIK
     RFIRQEIIKM FDERMAYYTS RMQFPMEMAA APGRPGPPGK DGAPGRPGAP GSPGLPGQIG
     REGRQGLPGV RGLPGTKGEK GDIGIGIAGE NGLPGPPGPQ GPPGYGKMGA TGPMGQQGIP
     GIPGPPGPMG QPGKAGHCNP SDCFGAMPME QQYPPMKTMK GPFG
//