VITRN_MOUSE
ID VITRN_MOUSE Reviewed; 650 AA.
AC Q8VHI5; Q3TZ47; Q8BQ41; Q8K047; Q9CYZ1;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Vitrin;
DE AltName: Full=Akhirin {ECO:0000303|PubMed:25331329};
DE Flags: Precursor;
GN Name=Vit; Synonyms=Akh {ECO:0000303|PubMed:25331329};
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 [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ;
RX PubMed=10830112; DOI=10.1042/bst0270832;
RA Mayne R., Ren Z.-X., Liu J.G., Cook T., Carson M., Narayana S.;
RT "VIT-1: the second member of a new branch of the von Willebrand factor A
RT domain superfamily.";
RL Biochem. Soc. Trans. 27:832-835(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Inner ear, and Spinal ganglion;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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, SUBUNIT, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=18757743; DOI=10.1073/pnas.0803640105;
RA Manabe R., Tsutsui K., Yamada T., Kimura M., Nakano I., Shimono C.,
RA Sanzen N., Furutani Y., Fukuda T., Oguri Y., Shimamoto K., Kiyozumi D.,
RA Sato Y., Sado Y., Senoo H., Yamashina S., Fukuda S., Kawai J., Sugiura N.,
RA Kimata K., Hayashizaki Y., Sekiguchi K.;
RT "Transcriptome-based systematic identification of extracellular matrix
RT proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:12849-12854(2008).
RN [5]
RP DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, INDUCTION, AND FUNCTION.
RX PubMed=25331329; DOI=10.1002/dneu.22238;
RA Abdulhaleem F.A., Song X., Kawano R., Uezono N., Ito A., Ahmed G.,
RA Hossain M., Nakashima K., Tanaka H., Ohta K.;
RT "Akhirin regulates the proliferation and differentiation of neural stem
RT cells in intact and injured mouse spinal cord.";
RL Dev. Neurobiol. 75:494-504(2015).
CC -!- FUNCTION: Promotes matrix assembly and cell adhesiveness
CC (PubMed:18757743). Plays a role in spinal cord formation by regulating
CC the proliferation and differentiation of neural stem cells
CC (PubMed:25331329). {ECO:0000269|PubMed:18757743,
CC ECO:0000269|PubMed:25331329}.
CC -!- SUBUNIT: Binds dermatan sulfate and chondroitin sulfate.
CC {ECO:0000269|PubMed:18757743}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:18757743}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VHI5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VHI5-2; Sequence=VSP_020212;
CC -!- DEVELOPMENTAL STAGE: At 16.5 dpc, present in skull base cartilage (at
CC protein level) (PubMed:18757743). Expressed in the floor plate as early
CC as 9.5 dpc and shifted to the central canal area from 13.5 dpc. At 15.5
CC dpc, the expression is restricted to the ventral midline region
CC (PubMed:25331329). {ECO:0000269|PubMed:18757743,
CC ECO:0000269|PubMed:25331329}.
CC -!- INDUCTION: Highly up-regulated in the injured spinal cord.
CC {ECO:0000269|PubMed:25331329}.
CC -!- DISRUPTION PHENOTYPE: Embryos show decreased spinal cord size
CC associated with reduced cell proliferation and altered cell
CC differentiation in the central canal of the neural tube.
CC {ECO:0000269|PubMed:25331329}.
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DR EMBL; AF454755; AAL57848.1; -; mRNA.
DR EMBL; AK013193; BAB28702.1; -; mRNA.
DR EMBL; AK051606; BAC34688.1; -; mRNA.
DR EMBL; AK158117; BAE34363.1; -; mRNA.
DR EMBL; BC034120; AAH34120.1; -; mRNA.
DR CCDS; CCDS37696.1; -. [Q8VHI5-1]
DR CCDS; CCDS89157.1; -. [Q8VHI5-2]
DR RefSeq; NP_001183957.1; NM_001197028.1.
DR RefSeq; NP_083089.1; NM_028813.2. [Q8VHI5-1]
DR AlphaFoldDB; Q8VHI5; -.
DR SMR; Q8VHI5; -.
DR BioGRID; 216570; 3.
DR STRING; 10090.ENSMUSP00000024880; -.
DR GlyGen; Q8VHI5; 1 site.
DR iPTMnet; Q8VHI5; -.
DR PhosphoSitePlus; Q8VHI5; -.
DR MaxQB; Q8VHI5; -.
DR PaxDb; Q8VHI5; -.
DR PRIDE; Q8VHI5; -.
DR ProteomicsDB; 297924; -. [Q8VHI5-1]
DR ProteomicsDB; 297925; -. [Q8VHI5-2]
DR Antibodypedia; 29304; 59 antibodies from 15 providers.
DR DNASU; 74199; -.
DR Ensembl; ENSMUST00000024880; ENSMUSP00000024880; ENSMUSG00000024076. [Q8VHI5-1]
DR GeneID; 74199; -.
DR KEGG; mmu:74199; -.
DR UCSC; uc008dox.2; mouse. [Q8VHI5-1]
DR UCSC; uc012axj.1; mouse. [Q8VHI5-2]
DR CTD; 5212; -.
DR MGI; MGI:1921449; Vit.
DR VEuPathDB; HostDB:ENSMUSG00000024076; -.
DR eggNOG; KOG1216; Eukaryota.
DR GeneTree; ENSGT00940000159330; -.
DR HOGENOM; CLU_019512_0_0_1; -.
DR InParanoid; Q8VHI5; -.
DR OMA; KTCFNSA; -.
DR OrthoDB; 200139at2759; -.
DR PhylomeDB; Q8VHI5; -.
DR TreeFam; TF318242; -.
DR BioGRID-ORCS; 74199; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Vit; mouse.
DR PRO; PR:Q8VHI5; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8VHI5; protein.
DR Bgee; ENSMUSG00000024076; Expressed in epithelium of lens and 149 other tissues.
DR ExpressionAtlas; Q8VHI5; baseline and differential.
DR Genevisible; Q8VHI5; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005614; C:interstitial matrix; IDA:MGI.
DR GO; GO:0005539; F:glycosaminoglycan binding; IDA:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IDA:MGI.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IDA:MGI.
DR GO; GO:0021510; P:spinal cord development; IMP:UniProtKB.
DR Gene3D; 2.170.130.20; -; 1.
DR Gene3D; 3.40.50.410; -; 2.
DR InterPro; IPR004043; LCCL.
DR InterPro; IPR036609; LCCL_sf.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF03815; LCCL; 1.
DR Pfam; PF00092; VWA; 2.
DR SMART; SM00603; LCCL; 1.
DR SMART; SM00327; VWA; 2.
DR SUPFAM; SSF53300; SSF53300; 2.
DR SUPFAM; SSF69848; SSF69848; 1.
DR PROSITE; PS50820; LCCL; 1.
DR PROSITE; PS50234; VWFA; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Neurogenesis; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..650
FT /note="Vitrin"
FT /id="PRO_0000248211"
FT DOMAIN 40..133
FT /note="LCCL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00123"
FT DOMAIN 265..450
FT /note="VWFA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 467..640
FT /note="VWFA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REGION 198..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 492
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 46..62
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00123"
FT DISULFID 66..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00123"
FT VAR_SEQ 18..39
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020212"
FT CONFLICT 6
FT /note="P -> L (in Ref. 1; AAL57848 and 2; BAE34363)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="T -> A (in Ref. 2; BAC34688)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="I -> V (in Ref. 2; BAE34363)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="Q -> R (in Ref. 1; AAL57848 and 2; BAE34363)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="V -> A (in Ref. 1; AAL57848 and 2; BAE34363)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="S -> P (in Ref. 1; AAL57848 and 2; BAE34363)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="N -> S (in Ref. 1; AAL57848 and 2; BAE34363)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="S -> G (in Ref. 1; AAL57848 and 2; BAE34363)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="Q -> K (in Ref. 2; BAE34363)"
FT /evidence="ECO:0000305"
FT CONFLICT 408..409
FT /note="DI -> EK (in Ref. 1; AAL57848 and 2; BAE34363)"
FT /evidence="ECO:0000305"
FT CONFLICT 416
FT /note="G -> V (in Ref. 1; AAL57848)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="M -> V (in Ref. 1; AAL57848 and 2; BAE34363)"
FT /evidence="ECO:0000305"
FT CONFLICT 518
FT /note="E -> Q (in Ref. 1; AAL57848)"
FT /evidence="ECO:0000305"
FT CONFLICT 589
FT /note="Y -> C (in Ref. 2; BAB28702)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 650 AA; 70699 MW; 1641623E11003B4E CRC64;
MGIVVPTMKA SVIEVLLVLL VTGIHSNKET PKKTKRPKLT VPQINCDVKA GKIINPEFMV
KCPAGCQDPK YHVYGTGVYA SYSSVCGAAI HSGVLDNSGG KILVRKVAGQ SGYKGSYSNG
VQSLSLPRWR ESFIVAESKP QKGVAYPSTL TYSSSKTAAA KAGETTKAYE KPSIPGTTIQ
PVTLTQAQAT PVAEVTHRST SKPFAASVTN SPRPQPVGHR SQEMEEVDGW KPGPVLLDSG
FVPKEELSTQ SSEPVPQGDP NCKIDLSFLI DGSTSIGKRR FRIQKQFLAD VVQALDIGPA
GPLVGVVQYG DNPATQFNLK THMNSQDLKT AIEKITQRGG LSNVGRAISF VTKTFFSKAN
GNRGGAPNVA VVMVDGWPTD KVEEVSRVAR ESGINVFFIT VEGAAERDIQ HVVEPGFASK
AVCRTNGFYS FNVQSWLSLH KTVQPLVKRV CDTDRLACSK TCLNSADIGF VIDGSSSMGT
SNFRTVLQFV ANLSKEFEIS DTDTRVGAVQ YTYEQRLEFG FDKYNSKADI LSAIRRVGYW
SGGTSTGAAI QYALEQLFKK SKPNKRKVMI IITDGRSYDD VRIPAMAAYQ KGVITYAIGI
AWAAQDELEV MATHPAKDHS FFVDDFDNLY KIAPRIIQNI CTEFNSQPRN
