(data stored in ACNUC22828 zone)

HOGENOM: HSX_PE126

ID   HSX_PE126                            STANDARD;      PRT;   680 AA.
AC   HSX_PE126; P23352; B2RPF8;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Anosmin-1;AltName: Full=Adhesion molecule-like
DE   X-linked;AltName: Full=Kallmann syndrome protein;Flags: Precursor;
DE   (HSX.PE126).
GN   Name=KAL1; Synonyms=ADMLX, KAL, KALIG1;
OS   HOMO SAPIENS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Primates; Haplorrhini; Simiiformes; Catarrhini;
OC   Hominoidea; Hominidae; Homininae; Homo.
OX   NCBI_TaxID=9606;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HSX.PE126.
CC       Homo sapiens chromosome X GRCh37  sequence 1..155260560 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:KALM_HUMAN
CC   -!- FUNCTION: Has a dual branch-promoting and guidance activity, which
CC       may play an important role in the patterning of mitral and tufted
CC       cell collaterals to the olfactory cortex (By similarity).
CC       Chemoattractant for fetal olfactory epithelial cells.
CC   -!- SUBUNIT: Interacts with FGFR1; this interaction does not interfere
CC       with FGF2-binding to FGFR1. Binds heparin. Heparin may promote or
CC       interfere with KAL1-FGFR1-FGF2 complex formation depending on the
CC       sequential order of its binding to the various constituents. For
CC       instance, heparin-KAL1 interaction favors subsequent binding to
CC       pre-existing binary FGFR1-FGF2 complex, while heparin-FGF2 complex
CC       does not interact with KAL1-FGFR1.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC       Secreted. Note=Proteolytic cleavage may release it from the cell
CC       surface into the extracellular space.
CC   -!- TISSUE SPECIFICITY: Expressed in the cerebellum (at protein
CC       level).
CC   -!- PTM: N-glycosylated.
CC   -!- PTM: May be proteolytically cleaved at the cell surface and
CC       released from the cell surface.
CC   -!- DISEASE: Defects in KAL1 are the cause of Kallmann syndrome type 1
CC       (KAL1) [MIM:308700]; also known as hypogonadotropic hypogonadism
CC       and anosmia. Anosmia or hyposmia is related to the absence or
CC       hypoplasia of the olfactory bulbs and tracts. Hypogonadism is due
CC       to deficiency in gonadotropin-releasing hormone and probably
CC       results from a failure of embryonic migration of gonadotropin-
CC       releasing hormone-synthesizing neurons. In some patients other
CC       developmental anomalies can be present, which include renal
CC       agenesis, cleft lip and/or palate, selective tooth agenesis, and
CC       bimanual synkinesis. In some cases anosmia may be absent or
CC       inconspicuous.
CC   -!- SIMILARITY: Contains 4 fibronectin type-III domains.
CC   -!- SIMILARITY: Contains 1 WAP domain.
CC   -!- WEB RESOURCE: Name=GeneReviews;
CC       URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/KAL1";
CC   -!- GENE_FAMILY: HOG000113190 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Homo_sapiens;ENSG00000011201;ENST00000262648;ENSP00000262648.
DR   EMBL; AC005184; - ;
DR   EMBL; AC006062; - ;
DR   EMBL; AC096511; - ;
DR   EMBL; BC137426; - ;
DR   EMBL; BC137427; - ;
DR   EMBL; CH471074; - ;
DR   EMBL; M97252; - ;
DR   EMBL; S60085; - ;
DR   EMBL; X60299; - ;
DR   EMBL; X82034; - ;
DR   UniProtKB/Swiss-Prot; P23352; B2RPF8; -.
DR   EMBL; M97252; AAA59202.1; -; mRNA.
DR   EMBL; S60085; AAB20108.1; ALT_SEQ; mRNA.
DR   EMBL; X60299; CAA42841.1; -; mRNA.
DR   EMBL; AC005184; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC006062; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC096511; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471074; EAW98759.1; -; Genomic_DNA.
DR   EMBL; BC137426; AAI37427.1; -; mRNA.
DR   EMBL; BC137427; AAI37428.1; -; mRNA.
DR   EMBL; X82034; CAA57554.1; -; Genomic_DNA.
DR   IPI; IPI00011174; -.
DR   PIR; A40351; A40351.
DR   PIR; S17982; S17982.
DR   RefSeq; NP_000207.2; NM_000216.2.
DR   UniGene; Hs.521869; -.
DR   PDB; 1ZLG; X-ray; -; A=24-680.
DR   PDBsum; 1ZLG; -.
DR   ProteinModelPortal; P23352; -.
DR   SMR; P23352; 128-176, 245-276, 289-383, 439-521, 548-656.
DR   STRING; P23352; -.
DR   PhosphoSite; P23352; -.
DR   PRIDE; P23352; -.
DR   Ensembl; ENST00000262648; ENSP00000262648; ENSG00000011201.
DR   GeneID; 3730; -.
DR   KEGG; hsa:3730; -.
DR   NMPDR; fig|9606.3.peg.32416; -.
DR   UCSC; uc004csf.1; human.
DR   CTD; 3730; -.
DR   GeneCards; GC0XM006324; -.
DR   H-InvDB; HIX0056280; -.
DR   HGNC; HGNC:6211; KAL1.
DR   MIM; 300836; gene.
DR   MIM; 308700; phenotype.
DR   neXtProt; NX_P23352; -.
DR   Orphanet; 478; Kallmann syndrome.
DR   PharmGKB; PA30012; -.
DR   eggNOG; prNOG16515; -.
DR   GeneTree; ENSGT00440000033720; -.
DR   InParanoid; P23352; -.
DR   OMA; PKNLYKG; -.
DR   OrthoDB; EOG45QHCR; -.
DR   PhylomeDB; P23352; -.
DR   NextBio; 14603; -.
DR   ArrayExpress; P23352; -.
DR   Bgee; P23352; -.
DR   CleanEx; HS_KAL1; -.
DR   Genevestigator; P23352; -.
DR   GermOnline; ENSG00000011201; Homo sapiens.
DR   GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005578; C:proteinaceous extracellular matrix; TAS:ProtInc.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; TAS:ProtInc.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007411; P:axon guidance; TAS:ProtInc.
DR   GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR   GO; GO:0006928; P:cellular component movement; TAS:ProtInc.
DR   InterPro; IPR015874; 4-disulphide_core.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR008197; Whey_acidic_protein_4-diS_core.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 3.
DR   Gene3D; G3DSA:4.10.75.10; Whey_acidic_protein_4-diS_core; 1.
DR   Pfam; PF00041; fn3; 3.
DR   Pfam; PF00095; WAP; 1.
DR   PRINTS; PR00003; 4DISULPHCORE.
DR   SMART; SM00060; FN3; 4.
DR   SMART; SM00217; WAP; 1.
DR   SUPFAM; SSF49265; FN_III-like; 3.
DR   SUPFAM; SSF57256; WAP; 1.
DR   PROSITE; PS50853; FN3; 4.
DR   PROSITE; PS51390; WAP; 1.
DR   HOGENOMDNA; HSX.PE126; -.
KW   ENSG000000112011755old_1320000031; ENSP000002626487901old_1320000031;
KW   AC005184; AC006062; AC096511; BC137426; BC137427; CH471074; M97252;
KW   X60299; X82034;
KW   3D-structure; Cell adhesion; Cell membrane; Chemotaxis;
KW   Complete proteome; Disease mutation; Glycoprotein; Heparin-binding;
KW   Hypogonadotropic hypogonadism; Kallmann syndrome; Membrane;
KW   Polymorphism; Protease inhibitor; Reference proteome; Repeat;
KW   Secreted; Serine protease inhibitor; Signal.
SQ   SEQUENCE   680 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MVPGVPGAVL TLCLWLAASS GCLAAGPGAA AARRLDESLS AGSVQRARCA SRCLSLQITR
     ISAFFQHFQN NGSLVWCQNH KQCSKCLEPC KESGDLRKHQ CQSFCEPLFP KKSYECLTSC
     EFLKYILLVK QGDCPAPEKA SGFAAACVES CEVDNECSGV KKCCSNGCGH TCQVPKTLYK
     GVPLKPRKEL RFTELQSGQL EVKWSSKFNI SIEPVIYVVQ RRWNYGIHPS EDDATHWQTV
     AQTTDERVQL TDIRPSRWYQ FRVAAVNVHG TRGFTAPSKH FRSSKDPSAP PAPANLRLAN
     STVNSDGSVT VTIVWDLPEE PDIPVHHYKV FWSWMVSSKS LVPTKKKRRK TTDGFQNSVI
     LEKLQPDCDY VVELQAITYW GQTRLKSAKV SLHFTSTHAT NNKEQLVKTR KGGIQTQLPF
     QRRRPTRPLE VGAPFYQDGQ LQVKVYWKKT EDPTVNRYHV RWFPEACAHN RTTGSEASSG
     MTHENYIILQ DLSFSCKYKV TVQPIRPKSH SKAEAVFFTT PPCSALKGKS HKPVGCLGEA
     GHVLSKVLAK PENLSASFIV QDVNITGHFS WKMAKANLYQ PMTGFQVTWA EVTTESRQNS
     LPNSIISQSQ ILPSDHYVLT VPNLRPSTLY RLEVQVLTPG GEGPATIKTF RTPELPPSSA
     HRSHLKHRHP HHYKPSPERY
//

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