F13B_HUMAN
ID F13B_HUMAN Reviewed; 661 AA.
AC P05160; A8K3E5; Q5VYL5;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 3.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Coagulation factor XIII B chain;
DE AltName: Full=Fibrin-stabilizing factor B subunit;
DE AltName: Full=Protein-glutamine gamma-glutamyltransferase B chain;
DE AltName: Full=Transglutaminase B chain;
DE Flags: Precursor;
GN Name=F13B;
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 [GENOMIC DNA], AND VARIANT HIS-115.
RX PubMed=2271707; DOI=10.1021/bi00503a007;
RA Bottenus R.E., Ichinose A., Davie E.W.;
RT "Nucleotide sequence of the gene for the b subunit of human factor XIII.";
RL Biochemistry 29:11195-11209(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-661, PROTEIN SEQUENCE OF N-TERMINUS, AND
RP VARIANT HIS-115.
RX PubMed=3021194; DOI=10.1021/bi00364a027;
RA Ichinose A., McMullen B.A., Fujikawa K., Davie E.W.;
RT "Amino acid sequence of the b subunit of human factor XIII, a protein
RT composed of ten repetitive segments.";
RL Biochemistry 25:4633-4638(1986).
RN [3]
RP SEQUENCE REVISION.
RA Ichinose A.;
RL Submitted (FEB-1987) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLU-569.
RC TISSUE=Heart;
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-115; THR-342; ARG-350;
RP PRO-529 AND GLU-569.
RG SeattleSNPs variation discovery resource;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-20.
RC TISSUE=Liver;
RX PubMed=2339067; DOI=10.1093/nar/18.9.2817;
RA Grundmann U., Nerlich C., Rein T., Zettlmeissl G.;
RT "Complete cDNA sequence encoding the B subunit of human factor XIII.";
RL Nucleic Acids Res. 18:2817-2817(1990).
RN [8]
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=4405643; DOI=10.1016/s0021-9258(19)44312-3;
RA Schwartz M.L., Pizzo S.V., Hill R.L., McKee P.A.;
RT "Human Factor XIII from plasma and platelets. Molecular weights, subunit
RT structures, proteolytic activation, and cross-linking of fibrinogen and
RT fibrin.";
RL J. Biol. Chem. 248:1395-1407(1973).
RN [9]
RP INVOLVEMENT IN FA13BD.
RX PubMed=11313256; DOI=10.1182/blood.v97.9.2667;
RA Koseki S., Souri M., Koga S., Yamakawa M., Shichishima T., Maruyama Y.,
RA Yanai F., Ichinose A.;
RT "Truncated mutant B subunit for factor XIII causes its deficiency due to
RT impaired intracellular transportation.";
RL Blood 97:2667-2672(2001).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-545.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-162.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [12]
RP REVIEW.
RX PubMed=21742792; DOI=10.1152/physrev.00016.2010;
RA Muszbek L., Bereczky Z., Bagoly Z., Komaromi I., Katona E.;
RT "Factor XIII: a coagulation factor with multiple plasmatic and cellular
RT functions.";
RL Physiol. Rev. 91:931-972(2011).
RN [13]
RP VARIANT FA13BD PHE-450.
RX PubMed=8324218;
RA Hashiguchi T., Saito M., Morishita E., Matsuda T., Ichinose A.;
RT "Two genetic defects in a patient with complete deficiency of the b-subunit
RT for coagulation factor XIII.";
RL Blood 82:145-150(1993).
RN [14]
RP VARIANTS VAL-49; HIS-115; ARG-350; VAL-388; SER-543 AND GLU-569.
RX PubMed=10391209; DOI=10.1038/10290;
RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA Lander E.S.;
RT "Characterization of single-nucleotide polymorphisms in coding regions of
RT human genes.";
RL Nat. Genet. 22:231-238(1999).
RN [15]
RP ERRATUM OF PUBMED:10391209.
RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA Lander E.S.;
RL Nat. Genet. 23:373-373(1999).
RN [16]
RP VARIANTS FA13BD ARG-25; ASN-101; PHE-136; ILE-237; PHE-336; GLU-421 AND
RP SER-448.
RX PubMed=20331752; DOI=10.1111/j.1365-2516.2010.02207.x;
RA Ivaskevicius V., Biswas A., Loreth R., Schroeder V., Ohlenforst S.,
RA Rott H., Krause M., Kohler H.P., Scharrer I., Oldenburg J.;
RT "Mutations affecting disulphide bonds contribute to a fairly common
RT prevalence of F13B gene defects: results of a genetic study in 14 families
RT with factor XIII B deficiency.";
RL Haemophilia 16:675-682(2010).
RN [17]
RP CHARACTERIZATION OF VARIANTS FA13BD ARG-25; ASN-101; PHE-136; ILE-237;
RP PHE-336; GLU-421 AND SER-448, SUBCELLULAR LOCATION, SUBUNIT, AND
RP INTERACTION WITH F13A1.
RX PubMed=26247044; DOI=10.1002/mgg3.138;
RA Thomas A., Biswas A., Ivaskevicius V., Oldenburg J.;
RT "Structural and functional influences of coagulation factor XIII subunit B
RT heterozygous missense mutants.";
RL Mol. Genet. Genomic Med. 3:258-271(2015).
CC -!- FUNCTION: The B chain of factor XIII is not catalytically active, but
CC is thought to stabilize the A subunits and regulate the rate of
CC transglutaminase formation by thrombin. {ECO:0000303|PubMed:21742792,
CC ECO:0000303|PubMed:3021194}.
CC -!- SUBUNIT: Tetramer of two A chains (F13A1) and two B (F13B) chains.
CC {ECO:0000269|PubMed:26247044, ECO:0000269|PubMed:4405643}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26247044,
CC ECO:0000269|PubMed:4405643}.
CC -!- DISEASE: Factor XIII subunit B deficiency (FA13BD) [MIM:613235]: An
CC autosomal recessive hematologic disorder characterized by a life-long
CC bleeding tendency, impaired wound healing and spontaneous abortion in
CC affected women. {ECO:0000269|PubMed:11313256,
CC ECO:0000269|PubMed:20331752, ECO:0000269|PubMed:26247044,
CC ECO:0000269|PubMed:8324218}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Factor XIII entry;
CC URL="https://en.wikipedia.org/wiki/Factor_XIII";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/f13b/";
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DR EMBL; M64554; AAA51821.1; -; Genomic_DNA.
DR EMBL; M14057; AAA88042.1; -; mRNA.
DR EMBL; AK290560; BAF83249.1; -; mRNA.
DR EMBL; AY692223; AAT85802.1; -; Genomic_DNA.
DR EMBL; AL353809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X51823; CAA36123.1; -; mRNA.
DR CCDS; CCDS1388.1; -.
DR PIR; A36397; KFHU13.
DR RefSeq; NP_001985.2; NM_001994.2.
DR AlphaFoldDB; P05160; -.
DR SMR; P05160; -.
DR BioGRID; 108463; 2.
DR ComplexPortal; CPX-6231; Coagulation factor XIIIa complex.
DR IntAct; P05160; 11.
DR STRING; 9606.ENSP00000356382; -.
DR ChEMBL; CHEMBL3351193; -.
DR DrugBank; DB09310; Catridecacog.
DR DrugBank; DB11571; Human thrombin.
DR DrugBank; DB11300; Thrombin.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR GlyConnect; 1122; 8 N-Linked glycans (2 sites).
DR GlyGen; P05160; 3 sites, 15 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
DR iPTMnet; P05160; -.
DR PhosphoSitePlus; P05160; -.
DR BioMuta; F13B; -.
DR DMDM; 145559473; -.
DR EPD; P05160; -.
DR MassIVE; P05160; -.
DR PaxDb; P05160; -.
DR PeptideAtlas; P05160; -.
DR PRIDE; P05160; -.
DR ProteomicsDB; 51808; -.
DR Antibodypedia; 868; 241 antibodies from 25 providers.
DR DNASU; 2165; -.
DR Ensembl; ENST00000367412.2; ENSP00000356382.2; ENSG00000143278.5.
DR GeneID; 2165; -.
DR KEGG; hsa:2165; -.
DR MANE-Select; ENST00000367412.2; ENSP00000356382.2; NM_001994.3; NP_001985.2.
DR UCSC; uc001gtt.1; human.
DR CTD; 2165; -.
DR DisGeNET; 2165; -.
DR GeneCards; F13B; -.
DR HGNC; HGNC:3534; F13B.
DR HPA; ENSG00000143278; Tissue enriched (liver).
DR MalaCards; F13B; -.
DR MIM; 134580; gene+phenotype.
DR MIM; 613235; phenotype.
DR neXtProt; NX_P05160; -.
DR OpenTargets; ENSG00000143278; -.
DR Orphanet; 331; Congenital factor XIII deficiency.
DR PharmGKB; PA27944; -.
DR VEuPathDB; HostDB:ENSG00000143278; -.
DR eggNOG; ENOG502RDCS; Eukaryota.
DR GeneTree; ENSGT00940000154967; -.
DR HOGENOM; CLU_020107_6_0_1; -.
DR InParanoid; P05160; -.
DR OMA; PLCVRKE; -.
DR OrthoDB; 296899at2759; -.
DR PhylomeDB; P05160; -.
DR TreeFam; TF326157; -.
DR PathwayCommons; P05160; -.
DR Reactome; R-HSA-140875; Common Pathway of Fibrin Clot Formation.
DR SignaLink; P05160; -.
DR BioGRID-ORCS; 2165; 7 hits in 1057 CRISPR screens.
DR GeneWiki; F13B; -.
DR GenomeRNAi; 2165; -.
DR Pharos; P05160; Tbio.
DR PRO; PR:P05160; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P05160; protein.
DR Bgee; ENSG00000143278; Expressed in right lobe of liver and 32 other tissues.
DR ExpressionAtlas; P05160; baseline and differential.
DR Genevisible; P05160; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IC:ComplexPortal.
DR GO; GO:1990234; C:transferase complex; IC:ComplexPortal.
DR GO; GO:0007596; P:blood coagulation; IBA:GO_Central.
DR GO; GO:0072378; P:blood coagulation, fibrin clot formation; IDA:ComplexPortal.
DR GO; GO:0018149; P:peptide cross-linking; IDA:ComplexPortal.
DR CDD; cd00033; CCP; 7.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR Pfam; PF00084; Sushi; 8.
DR SMART; SM00032; CCP; 8.
DR SUPFAM; SSF57535; SSF57535; 10.
DR PROSITE; PS50923; SUSHI; 7.
PE 1: Evidence at protein level;
KW Blood coagulation; Direct protein sequencing; Disease variant;
KW Disulfide bond; Glycoprotein; Hemostasis; Reference proteome; Repeat;
KW Secreted; Signal; Sushi.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:3021194"
FT CHAIN 21..661
FT /note="Coagulation factor XIII B chain"
FT /id="PRO_0000021222"
FT DOMAIN 24..88
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 89..148
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 151..210
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 211..269
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 272..329
FT /note="Sushi 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 334..391
FT /note="Sushi 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 394..452
FT /note="Sushi 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 453..516
FT /note="Sushi 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 522..580
FT /note="Sushi 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 581..647
FT /note="Sushi 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT MOTIF 617..619
FT /note="Cell attachment site"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 545
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT DISULFID 25..76
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 59..87
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 91..135
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 118..146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 153..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 180..208
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 213..255
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 241..267
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 274..316
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 302..327
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 336..378
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 364..389
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 396..439
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 425..450
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 454..505
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 486..515
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 524..567
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 553..578
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 582..636
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 616..646
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT VARIANT 25
FT /note="C -> R (in FA13BD; may disrupt a disulfide bond;
FT impaired subcellular location leading to accumulation in
FT the endoplasmic reticulum; impaired interaction with F13A1;
FT impaired structure; dbSNP:rs1232302447)"
FT /evidence="ECO:0000269|PubMed:20331752,
FT ECO:0000269|PubMed:26247044"
FT /id="VAR_074563"
FT VARIANT 49
FT /note="M -> V (in dbSNP:rs6002)"
FT /evidence="ECO:0000269|PubMed:10391209"
FT /id="VAR_013930"
FT VARIANT 101
FT /note="I -> N (in FA13BD; impaired interaction with F13A1;
FT dbSNP:rs753009140)"
FT /evidence="ECO:0000269|PubMed:20331752,
FT ECO:0000269|PubMed:26247044"
FT /id="VAR_074564"
FT VARIANT 115
FT /note="R -> H (in dbSNP:rs6003)"
FT /evidence="ECO:0000269|PubMed:10391209,
FT ECO:0000269|PubMed:2271707, ECO:0000269|PubMed:3021194,
FT ECO:0000269|Ref.5"
FT /id="VAR_013931"
FT VARIANT 136
FT /note="L -> F (in FA13BD; unknown pathological
FT significance; dbSNP:rs757094432)"
FT /evidence="ECO:0000269|PubMed:20331752,
FT ECO:0000269|PubMed:26247044"
FT /id="VAR_074565"
FT VARIANT 237
FT /note="V -> I (in FA13BD; unknown pathological
FT significance; dbSNP:rs145637157)"
FT /evidence="ECO:0000269|PubMed:20331752,
FT ECO:0000269|PubMed:26247044"
FT /id="VAR_074566"
FT VARIANT 336
FT /note="C -> F (in FA13BD; may disrupt a disulfide bond;
FT impaired interaction with F13A1; impaired structure;
FT dbSNP:rs778826479)"
FT /evidence="ECO:0000269|PubMed:20331752,
FT ECO:0000269|PubMed:26247044"
FT /id="VAR_074567"
FT VARIANT 342
FT /note="I -> T (in dbSNP:rs17514281)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_020612"
FT VARIANT 350
FT /note="H -> R (in dbSNP:rs5999)"
FT /evidence="ECO:0000269|PubMed:10391209, ECO:0000269|Ref.5"
FT /id="VAR_013932"
FT VARIANT 388
FT /note="E -> V (in dbSNP:rs5991)"
FT /evidence="ECO:0000269|PubMed:10391209"
FT /id="VAR_013933"
FT VARIANT 421
FT /note="V -> E (in FA13BD; impaired interaction with F13A1)"
FT /evidence="ECO:0000269|PubMed:20331752,
FT ECO:0000269|PubMed:26247044"
FT /id="VAR_074568"
FT VARIANT 448
FT /note="P -> S (in FA13BD; impaired interaction with F13A1;
FT impaired structure)"
FT /evidence="ECO:0000269|PubMed:20331752,
FT ECO:0000269|PubMed:26247044"
FT /id="VAR_074569"
FT VARIANT 450
FT /note="C -> F (in FA13BD; dbSNP:rs121913075)"
FT /evidence="ECO:0000269|PubMed:8324218"
FT /id="VAR_007475"
FT VARIANT 529
FT /note="L -> P (in dbSNP:rs17549671)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_020613"
FT VARIANT 543
FT /note="Y -> S (in dbSNP:rs6001)"
FT /evidence="ECO:0000269|PubMed:10391209"
FT /id="VAR_013934"
FT VARIANT 569
FT /note="D -> E (in dbSNP:rs6000)"
FT /evidence="ECO:0000269|PubMed:10391209,
FT ECO:0000269|PubMed:14702039, ECO:0000269|Ref.5"
FT /id="VAR_013935"
SQ SEQUENCE 661 AA; 75511 MW; 57A2FD2A0E35B812 CRC64;
MRLKNLTFII ILIISGELYA EEKPCGFPHV ENGRIAQYYY TFKSFYFPMS IDKKLSFFCL
AGYTTESGRQ EEQTTCTTEG WSPEPRCFKK CTKPDLSNGY ISDVKLLYKI QENMRYGCAS
GYKTTGGKDE EVVQCLSDGW SSQPTCRKEH ETCLAPELYN GNYSTTQKTF KVKDKVQYEC
ATGYYTAGGK KTEEVECLTY GWSLTPKCTK LKCSSLRLIE NGYFHPVKQT YEEGDVVQFF
CHENYYLSGS DLIQCYNFGW YPESPVCEGR RNRCPPPPLP INSKIQTHST TYRHGEIVHI
ECELNFEIHG SAEIRCEDGK WTEPPKCIEG QEKVACEEPP FIENGAANLH SKIYYNGDKV
TYACKSGYLL HGSNEITCNR GKWTLPPECV ENNENCKHPP VVMNGAVADG ILASYATGSS
VEYRCNEYYL LRGSKISRCE QGKWSSPPVC LEPCTVNVDY MNRNNIEMKW KYEGKVLHGD
LIDFVCKQGY DLSPLTPLSE LSVQCNRGEV KYPLCTRKES KGMCTSPPLI KHGVIISSTV
DTYENGSSVE YRCFDHHFLE GSREAYCLDG MWTTPPLCLE PCTLSFTEME KNNLLLKWDF
DNRPHILHGE YIEFICRGDT YPAELYITGS ILRMQCDRGQ LKYPRCIPRQ STLSYQEPLR
T
